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• W2014142786 abstract "S100A13, a member of the S100 gene family of Ca2+-binding proteins has been previously characterized as a component of a brain-derived heparin-binding multiprotein aggregate/complex containing fibroblast growth factor 1 (FGF1). We report that while expression of S100A13 in NIH 3T3 cells results in the constitutive release of S100A13 into the extracellular compartment at 37 °C, co-expression of S100A13 with FGF1 represses the constitutive release of S100A13 and enables NIH 3T3 cells to release S100A13 in response to temperature stress. S100A13 release in response to stress occurs with kinetics similar to that observed for the stress-induced release of FGF1, but S100A13 expression is able to reverse the sensitivity of FGF1 release to inhibitors of transcription and translation. The release of FGF1 and S100A13 in response to heat shock results in the solubility of FGF1 at 100% (w/v) ammonium sulfate saturation, and the expression of a S100A13 deletion mutant lacking its novel basic residue-rich domain acts as a dominant negative effector of FGF1 release in vitro. Surprisingly, the expression of S100A13 also results in the stress-induced release of a Cys-free FGF1 mutant, which is normally not released from NIH 3T3 cells in response to heat shock. These data suggest that S100A13 may be a component of the pathway for the release of the signal peptide-less polypeptide, FGF1, and may involve a role for S100A13 in the formation of a noncovalent FGF1 homodimer. S100A13, a member of the S100 gene family of Ca2+-binding proteins has been previously characterized as a component of a brain-derived heparin-binding multiprotein aggregate/complex containing fibroblast growth factor 1 (FGF1). We report that while expression of S100A13 in NIH 3T3 cells results in the constitutive release of S100A13 into the extracellular compartment at 37 °C, co-expression of S100A13 with FGF1 represses the constitutive release of S100A13 and enables NIH 3T3 cells to release S100A13 in response to temperature stress. S100A13 release in response to stress occurs with kinetics similar to that observed for the stress-induced release of FGF1, but S100A13 expression is able to reverse the sensitivity of FGF1 release to inhibitors of transcription and translation. The release of FGF1 and S100A13 in response to heat shock results in the solubility of FGF1 at 100% (w/v) ammonium sulfate saturation, and the expression of a S100A13 deletion mutant lacking its novel basic residue-rich domain acts as a dominant negative effector of FGF1 release in vitro. Surprisingly, the expression of S100A13 also results in the stress-induced release of a Cys-free FGF1 mutant, which is normally not released from NIH 3T3 cells in response to heat shock. These data suggest that S100A13 may be a component of the pathway for the release of the signal peptide-less polypeptide, FGF1, and may involve a role for S100A13 in the formation of a noncovalent FGF1 homodimer. fibroblast growth factor dithiothreitol endoplasmic reticulum interleukin polyacrylamide gel electrophoresis synaptotagmin FGF11 and FGF2 are the prototype members of a large family of heparin-binding growth factor genes that regulate numerous biological processes such as neurogenesis, mesoderm formation, and angiogenesis (1Burgess W.H. Maciag T. Annu. Rev. Biochem. 1989; 58: 575-606Crossref PubMed Google Scholar, 2Friesel R. Maciag T. Thromb. Haemostasis. 1999; 82: 748-754Crossref PubMed Scopus (90) Google Scholar). FGF1 and FGF2 lack a classical signal peptide sequence that provides access to the conventional endoplasmic reticulum (ER)-Golgi secretion pathway, a characteristic that led to the hypothesis that the release of these polypeptides may proceed through novel release/export pathways (2Friesel R. Maciag T. Thromb. Haemostasis. 1999; 82: 748-754Crossref PubMed Scopus (90) Google Scholar). Our laboratory previously demonstrated that FGF1, but not FGF2, is released as a latent homodimer by a transcription- and translation-dependent mechanism in response to a variety of cellular stresses including heat shock (3Jackson A. Friedman S. Zhan X. Engleka K.A. Forough R. Maciag T. Proc. Natl. Acad. Sci. U. S. A. 1992; 89: 10691-10695Crossref PubMed Scopus (225) Google Scholar), hypoxia (4Carreira, C. M., Landriscina, M., Bellum, S., Prudovsky, I., and Maciag, T. (2001) Growth Factors, in Press.Google Scholar), and serum starvation (5Shin J.T. Opalenik S.R. Wehby J.N. Mahesh V.K. Jackson A. Tarantini F. Maciag T. Thompson J.A. Biochim. Biophys. Acta. 1996; 1312: 27-38Crossref PubMed Scopus (78) Google Scholar). Conversely, the disruption of communication between the ER and Golgi apparatus by brefeldin A does not prevent the release of FGF1 from NIH 3T3 cells, confirming that FGF1 release may occur through a nonconventional pathway (6Jackson A. Tarantini F. Gamble S. Friedman S. Maciag T. J. Biol. Chem. 1995; 270: 33-36Abstract Full Text Full Text PDF PubMed Scopus (94) Google Scholar).FGF1 is released in vitro as a reducing agent- and denaturant-sensitive complex, which contains the p40 extravesicular domain of the Ca2+-binding protein, p65 synaptotagmin (Syt)1 (7Tarantini F. LaVallee T. Jackson A. Gamble S. Carreira C.M. Garfinkel S. Burgess W.H. Maciag T. J. Biol. Chem. 1998; 273: 22209-22216Abstract Full Text Full Text PDF PubMed Scopus (65) Google Scholar). The release of FGF1 in response to stress is dependent on Syt1 expression, since the expression of either a deletion mutant lacking 95 amino acids from the extravesicular portion of Syt1 or an antisense-Syt1 gene is able to repress FGF1 release in NIH 3T3 cells (7Tarantini F. LaVallee T. Jackson A. Gamble S. Carreira C.M. Garfinkel S. Burgess W.H. Maciag T. J. Biol. Chem. 1998; 273: 22209-22216Abstract Full Text Full Text PDF PubMed Scopus (65) Google Scholar, 8LaVallee T.M. Tarantini F. Gamble S. Carreira C.M. Jackson A. Maciag T. J. Biol. Chem. 1998; 273: 22217-22223Abstract Full Text Full Text PDF PubMed Scopus (67) Google Scholar). In addition, FGF1 purified from ovine brain as a high molecular weight aggregate exists as a component of a noncovalent heparin-binding complex with p40 Syt1 and S100A13 (9Carreira C.M. LaVallee T.M. Tarantini F. Jackson A. Lathrop J.T. Hampton B. Burgess W.H. Maciag T. J. Biol. Chem. 1998; 273: 22224-22231Abstract Full Text Full Text PDF PubMed Scopus (97) Google Scholar).The interleukin (IL)-1 gene family of proinflammatory polypeptides also contains functional cytokines that act as extracellular, receptor-dependent mediators of cellular function (10Dinarello C.A. Int. Rev. Immunol. 1998; 16: 457-499Crossref PubMed Scopus (671) Google Scholar, 11Smith D.E. Renshaw B.R. Ketchem R.R. Kubin M. Garka K.E. Sims J.E. J. Biol. Chem. 2000; 275: 1169-1175Abstract Full Text Full Text PDF PubMed Scopus (284) Google Scholar), yet the majority of the members of the IL-1 gene family lack a classical signal peptide sequence for conventional secretion (10Dinarello C.A. Int. Rev. Immunol. 1998; 16: 457-499Crossref PubMed Scopus (671) Google Scholar, 11Smith D.E. Renshaw B.R. Ketchem R.R. Kubin M. Garka K.E. Sims J.E. J. Biol. Chem. 2000; 275: 1169-1175Abstract Full Text Full Text PDF PubMed Scopus (284) Google Scholar). Interestingly, crystallographic analysis of the FGF and IL-1 prototypes demonstrates a remarkable level of structural similarity between these seemingly disparate polypeptides (12Thomas K.A. Rios-Candelore M. Gimenez-Gallego G. DiSalvo J. Bennett C. Rodkey J. Fitzpatrick S. Proc. Natl. Acad. Sci. U. S. A. 1985; 82: 6409-6413Crossref PubMed Scopus (222) Google Scholar, 13Zhang J.D. Cousens L.S. Barr P.J. Sprang S.R. Proc. Natl. Acad. Sci. U. S. A. 1991; 88: 3446-3450Crossref PubMed Scopus (223) Google Scholar). Recent studies have suggested that the pathway utilized for the release of IL-1α is quite similar yet distinct from the pathway utilized by FGF1 export, since both proteins are released in response to temperature stress with similar biochemical and pharmacologic properties (14Tarantini F. Micucci I. Bellum S. Landriscina M. Garfinkel S. Prudovsky I. Maciag T. J. Biol. Chem. 2001; 276: 5147-5151Abstract Full Text Full Text PDF PubMed Scopus (35) Google Scholar). In contrast, however, the IL-1α release pathway requires the proteolytic processing of the 31-kDa precursor form of IL-1α to the 17-kDa mature form for IL-1α release and does not appear to utilize Syt1 for export, since a dominant negative Syt1 mutant blocks FGF1 but not IL-1α release (14Tarantini F. Micucci I. Bellum S. Landriscina M. Garfinkel S. Prudovsky I. Maciag T. J. Biol. Chem. 2001; 276: 5147-5151Abstract Full Text Full Text PDF PubMed Scopus (35) Google Scholar). Although we have not been able to eliminate the function of other Syt gene family members in the stress-induced release of IL-1α, the observation that the precursor form of IL-1α is able to block the release of FGF1 in response to temperature stress suggests that the FGF1 and IL-1α release pathways may be mechanistically linked (14Tarantini F. Micucci I. Bellum S. Landriscina M. Garfinkel S. Prudovsky I. Maciag T. J. Biol. Chem. 2001; 276: 5147-5151Abstract Full Text Full Text PDF PubMed Scopus (35) Google Scholar).Recently, we have reported that amlexanox, an anti-allergic drug that binds S100A13 (15Shishibori T. Oyama Y. Matsushita O. Yamashita K. Furuichi H. Okabe A. Maeta H. Hata Y. Kobayashi R. Biochem. J. 1999; 338: 583-589Crossref PubMed Scopus (78) Google Scholar), is able to inhibit the release of FGF1 and p40 Syt1 in response to temperature stress (9Carreira C.M. LaVallee T.M. Tarantini F. Jackson A. Lathrop J.T. Hampton B. Burgess W.H. Maciag T. J. Biol. Chem. 1998; 273: 22224-22231Abstract Full Text Full Text PDF PubMed Scopus (97) Google Scholar, 16Landriscina M. Prudovsky I. Carreira C.M. Soldi R. Tarantini F. Maciag T. J. Biol. Chem. 2000; 275: 32753-32762Abstract Full Text Full Text PDF PubMed Scopus (36) Google Scholar). Because amlexanox also induces a Src-dependent and reversible disassembly of actin stress fibers (16Landriscina M. Prudovsky I. Carreira C.M. Soldi R. Tarantini F. Maciag T. J. Biol. Chem. 2000; 275: 32753-32762Abstract Full Text Full Text PDF PubMed Scopus (36) Google Scholar), these data have suggested a role for the actin cytoskeleton in the regulation of FGF1 release (16Landriscina M. Prudovsky I. Carreira C.M. Soldi R. Tarantini F. Maciag T. J. Biol. Chem. 2000; 275: 32753-32762Abstract Full Text Full Text PDF PubMed Scopus (36) Google Scholar).S100A13 is a member of a large gene family of Ca2+-binding proteins characterized by the absence of a classical signal peptide sequence and the presence of two Ca2+-binding EF-hand domains (17Donato R. Biochim. Biophys. Acta. 1999; 1450: 191-231Crossref PubMed Scopus (592) Google Scholar, 18Heizmann C.W. Cox J.A. Biometals. 1998; 11: 383-397Crossref PubMed Scopus (259) Google Scholar). S100A13 is a novel member of the S100 gene family that encodes a protein containing a positively charged carboxyl-terminal domain that may be involved in specific protein interactions (19Wicki R. Schafer B.W. Erne P. Heizmann C.W. Biochem. Biophys. Res. Commun. 1996; 227: 594-599Crossref PubMed Scopus (63) Google Scholar). While members of the S100 gene family, including S100A13 (20Ridinger K. Schafer B.W. Durussel I. Cox J.A. Heizmann C.W. J. Biol. Chem. 2000; 275: 8686-8694Abstract Full Text Full Text PDF PubMed Scopus (47) Google Scholar), are expressed in a variety of tissues and organs (17Donato R. Biochim. Biophys. Acta. 1999; 1450: 191-231Crossref PubMed Scopus (592) Google Scholar,18Heizmann C.W. Cox J.A. Biometals. 1998; 11: 383-397Crossref PubMed Scopus (259) Google Scholar), the expression of a few members of the S100 gene family have been implicated in the regulation of human pathology including neurodegenerative diseases, cardiomyopathies, cancer, and chronic inflammation (17Donato R. Biochim. Biophys. Acta. 1999; 1450: 191-231Crossref PubMed Scopus (592) Google Scholar, 18Heizmann C.W. Cox J.A. Biometals. 1998; 11: 383-397Crossref PubMed Scopus (259) Google Scholar). Interestingly, members of the S100 gene family have been shown to be constitutively released into the extracellular compartment (17Donato R. Biochim. Biophys. Acta. 1999; 1450: 191-231Crossref PubMed Scopus (592) Google Scholar, 18Heizmann C.W. Cox J.A. Biometals. 1998; 11: 383-397Crossref PubMed Scopus (259) Google Scholar, 21Rammes A. Roth J. Goebeler M. Klempt M. Hartmann M. Sorg C. J. Biol. Chem. 1997; 272: 9496-9502Abstract Full Text Full Text PDF PubMed Scopus (469) Google Scholar), where they have been characterized as leukocyte chemoattractants and regulators of macrophage activation (17Donato R. Biochim. Biophys. Acta. 1999; 1450: 191-231Crossref PubMed Scopus (592) Google Scholar,18Heizmann C.W. Cox J.A. Biometals. 1998; 11: 383-397Crossref PubMed Scopus (259) Google Scholar, 22Geczy C. Biochim. Biophys. Acta. 1996; 1313: 246-252Crossref PubMed Scopus (34) Google Scholar).Since S100A13 was purified from the ovine brain as a part of the multiprotein aggregate containing FGF1 and p40 Syt1, we sought to determine whether S100A13 is involved in the release of FGF1. We report that S100A13 expression facilitates the release of FGF1 into the extracellular compartment in response to temperature stress in vitro and that S100A13 expression is able to revert the dependence for both transcription and translation in the release of FGF1 in response to heat shock. We further describe the unanticipated observation that S100A13 expression is able to export a Cys-free FGF1 mutant, suggesting that S100A13 may be involved in the formation of the FGF1 homodimer, a prerequisite for export.DISCUSSIONOur data suggest that S100A13 is involved in the regulation of the stress-induced FGF1 release pathways. Thus, like the stress-induced release of FGF1 (3Jackson A. Friedman S. Zhan X. Engleka K.A. Forough R. Maciag T. Proc. Natl. Acad. Sci. U. S. A. 1992; 89: 10691-10695Crossref PubMed Scopus (225) Google Scholar), p40 Syt1 (7Tarantini F. LaVallee T. Jackson A. Gamble S. Carreira C.M. Garfinkel S. Burgess W.H. Maciag T. J. Biol. Chem. 1998; 273: 22209-22216Abstract Full Text Full Text PDF PubMed Scopus (65) Google Scholar, 8LaVallee T.M. Tarantini F. Gamble S. Carreira C.M. Jackson A. Maciag T. J. Biol. Chem. 1998; 273: 22217-22223Abstract Full Text Full Text PDF PubMed Scopus (67) Google Scholar), and murine IL-1α (14Tarantini F. Micucci I. Bellum S. Landriscina M. Garfinkel S. Prudovsky I. Maciag T. J. Biol. Chem. 2001; 276: 5147-5151Abstract Full Text Full Text PDF PubMed Scopus (35) Google Scholar), the stress-induced release of Myc-S100A13 is sensitive to agents that interfere with ATP biosynthesis and organization of the F-actin cytoskeleton but is insensitive to disruption of intracellular communication between the ER-Golgi apparatus. However, several observations suggest that S100A13, unlike p40 Syt1, is able to facilitate the release of FGF1. Indeed, expression of Myc-S100A13 was able to overcome the inhibitory activity of actinomycin and cycloheximide on FGF1 release and was able to induce the release of Cys-free FGF1 in response to stress, suggesting a functional role for S100A13 in the FGF1 release pathway as a potential modifier of a stress-induced post-translational event.The finding that Myc-S100A13 expression is able to overcome the requirement for transcription and translation in the release of FGF1 is consistent with the observation that some members of the S100 gene family have been characterized not only as stress-induced genes (36Andrejevic S. Bukilica M. Dimitrijevic M. Laban O. Radulovic J. Kovacevic-Jovanovic V. Stanojevic S. Vasiljevic T. Markovic B.M. Int. J. Neurosci. 1997; 89: 153-164Crossref PubMed Scopus (5) Google Scholar, 37Hoyaux D. Decaestecker C. Heizmann C.W. Vogl T. Schafer B.W. Salmon I. Kiss R. Pochet R. Brain Res. 2000; 867: 280-288Crossref PubMed Scopus (61) Google Scholar, 38Duarte W.R. Kasugai S. Iimura T. Oida S. Takenaga K. Ohya K. Ishikawa I. J. Dent. Res. 1998; 77: 1694-1699Crossref PubMed Scopus (23) Google Scholar, 39Hou X.E. Lundmark K. Dahlstrom A.B. J. Neurocytol. 1998; 27: 441-451Crossref PubMed Scopus (20) Google Scholar) but also as Cu2+-binding proteins (17Donato R. Biochim. Biophys. Acta. 1999; 1450: 191-231Crossref PubMed Scopus (592) Google Scholar, 18Heizmann C.W. Cox J.A. Biometals. 1998; 11: 383-397Crossref PubMed Scopus (259) Google Scholar, 40Nishikawa T. Lee I.S. Shiraishi N. Ishikawa T. Ohta Y. Nishikimi M. J. Biol. Chem. 1997; 272: 23037-23041Abstract Full Text Full Text PDF PubMed Scopus (80) Google Scholar,41Schafer B.W. Fritschy J.M. Murmann P. Troxler H. Durussel I. Heizmann C.W. Cox J.A. J. Biol. Chem. 2000; 275: 30623-30630Abstract Full Text Full Text PDF PubMed Scopus (77) Google Scholar). It is interesting to note that S100B was independently characterized from neural tissue as an inhibitor of Cu2+-mediated l-ascorbate oxidation (40Nishikawa T. Lee I.S. Shiraishi N. Ishikawa T. Ohta Y. Nishikimi M. J. Biol. Chem. 1997; 272: 23037-23041Abstract Full Text Full Text PDF PubMed Scopus (80) Google Scholar). Moreover, S100A4, S100A6, S100A7, and S100B are up-regulated in several human tumor cells, where they are associated with increased invasiveness of transformed cells and acquisition of metastatic phenotype (17Donato R. Biochim. Biophys. Acta. 1999; 1450: 191-231Crossref PubMed Scopus (592) Google Scholar). The murine analog of S100A8, the CP-10 protein, has been also associated with inflammation, since it is expressed and released in macrophages and endothelial cells only after their activation by interleukin-1 and lipopolysaccharide (17Donato R. Biochim. Biophys. Acta. 1999; 1450: 191-231Crossref PubMed Scopus (592) Google Scholar, 42Yen T. Harrison C.A. Devery J.M. Leong S. Iismaa S.E. Yoshimura T. Geczy C.L. Blood. 1997; 90: 4812-4821Crossref PubMed Google Scholar). However, the observation that the S100A13 gene is not induced in response to heat shock in NIH 3T3 cells does not eliminate the possibility that other members of the S100 gene family may participate in the release of FGF1 and that the expression of S100A13 may compensate for their function.While it is difficult to anticipate how S100A13 participates in these release pathways, we suggest that S100A13 may be able to orient FGF1 and Cys-free FGF1 in a manner that enables these polypeptides to form noncovalent homodimers. Indeed, Cu2+ oxidation is able to induce FGF1 homodimer (26Engleka K.A. Maciag T. J. Biol. Chem. 1992; 267: 11307-11315Abstract Full Text PDF PubMed Google Scholar) and FGF1 IL-1α heterodimer formation (26Engleka K.A. Maciag T. J. Biol. Chem. 1992; 267: 11307-11315Abstract Full Text PDF PubMed Google Scholar). Additional evidence from S100 crystallographic studies demonstrates that members of the S100 gene family are able to form stable Ca2+-independent homodimers and through an alteration in their conformation enable the two EF-hands in S100 to hold polypeptides, such as annexin 2 (Anx2) (43Kang H.M. Kassam G. Jarvis S.E. Fitzpatrick S.L. Waisman D.M. Biochemistry. 1997; 36: 2041-2050Crossref PubMed Scopus (41) Google Scholar), enabling the carboxyl-terminal domain of the polypeptide to interact with other proteins (17Donato R. Biochim. Biophys. Acta. 1999; 1450: 191-231Crossref PubMed Scopus (592) Google Scholar, 18Heizmann C.W. Cox J.A. Biometals. 1998; 11: 383-397Crossref PubMed Scopus (259) Google Scholar). In studies utilizing the interaction between S100A11 and Anx1 (44Seemann J. Weber K. Gerke V. Biochem. J. 1996; 319: 123-129Crossref PubMed Scopus (71) Google Scholar, 45Mailliard W.S. Haigler H.T. Schlaepfer D.D. J. Biol. Chem. 1996; 271: 719-725Abstract Full Text Full Text PDF PubMed Scopus (106) Google Scholar) as well as between S100A10 and Anx2 (43Kang H.M. Kassam G. Jarvis S.E. Fitzpatrick S.L. Waisman D.M. Biochemistry. 1997; 36: 2041-2050Crossref PubMed Scopus (41) Google Scholar), the orientation established by these conformational changes yields the formation of stable heterotetramers (S100A112·Anx12 and S100A102·Anx22). In the situations with FGF1, it is intriguing to speculate that S100A13 may be able to form similar heterotetramers with these polypeptides. Indeed, this may explain how S100A13 is able to facilitate the release of Cys-free FGF1, since it is possible that when interacting with native FGF1, S100A13 may be able to orient its conformation to expose Cys30, which is not exposed to solvent in its native conformation (46Blaber M. DiSalvo J. Thomas K.A. Biochemistry. 1996; 35: 2086-2094Crossref PubMed Scopus (125) Google Scholar), for FGF1 homodimer oxidation. In the absence of Cys30, S100A13 may enable Cys-free FGF1 to form the noncovalent equivalent of the FGF1 Cys30 homodimer as a component of a FGF2·S100A132 heterotetramer so that it can be released in response to heat shock. This would be consistent with the observation that the stress-induced release of Cys-free FGF1 and Myc-S100A13 exhibits similar kinetics and responsiveness to pharmacological agents including amlexanox, 2-deoxyglucose, brefeldin A, cycloheximide, and actinomycin D (data not shown). In addition, the S100A13-dependent increase in the solubility of Cys-free FGF1 under conditions of 100% (w/v) ammonium sulfate saturation also supports the premise that S100A13 may be able to associate with the monomeric form of FGF1 in response to temperature stress, and this association may involve the formation of a noncovalent heterotetramer complex that may enable Cys-free FGF1 to access the release pathway. Interestingly, the ability of S100A13 to force FGF1 into the supernatant fraction under conditions of saturated ammonium sulfate fractionation would be consistent with this suggestion, since solubility in ammonium sulfate is well described as being sensitive to alterations in protein conformation (47Das B.K. Agarwal S.K. Khan M.Y. Biochem. Int. 1992; 28: 775-781PubMed Google Scholar).It is interesting that latrunculin and amlexanox, which are known to attenuate the F-actin cytoskeleton (16Landriscina M. Prudovsky I. Carreira C.M. Soldi R. Tarantini F. Maciag T. J. Biol. Chem. 2000; 275: 32753-32762Abstract Full Text Full Text PDF PubMed Scopus (36) Google Scholar, 32Spector I. Schochet N.R. Blasberger D. Kashman Y. Cell Motil. Cytoskeleton. 1989; 13: 127-144Crossref PubMed Scopus (481) Google Scholar), also inhibit the heat shock-induced release of FGF1 and Myc-S100A13. Indeed, this suggests that the cytoskeleton may play an important role in the FGF1 release pathway. The premise is further supported by the association of the members of the S100 gene family with actin stress fibers, which is dependent upon the physiological status of the cell (48Mandinova A. Atar D. Schafer B.W. Spiess M. Aebi U. Heizmann C.W. J. Cell Sci. 1998; 111: 2043-2054Crossref PubMed Google Scholar). As a result, it is possible that S100A13 may act as an adaptor between FGF1 and F-actin structures. The F-actin cytoskeleton may be involved in at least two stages of the stress-induced release of FGF1 and Myc-S100A13: (i) the transport of the complex to the cell membrane proceeding along F-actin stress fibers with the potential participation of myosin molecular motors (49Mehta A.D. Rock R.S. Rief M. Spudich J.A. Mooseker M.S. Cheney R.E. Nature. 1999; 400: 590-593Crossref PubMed Scopus (670) Google Scholar) and (ii) exocytosis, which has been demonstrated to depend on the submembrane actin cortex during classical protein secretion (50Lang T. Wacker I. Wunderlich I. Rohrbach A. Giese G. Soldati T. Almers W. Biophys. J. 2000; 78: 2863-2877Abstract Full Text Full Text PDF PubMed Scopus (187) Google Scholar). Because both actin-dependent transport and exocytosis are energy-dependent processes (50Lang T. Wacker I. Wunderlich I. Rohrbach A. Giese G. Soldati T. Almers W. Biophys. J. 2000; 78: 2863-2877Abstract Full Text Full Text PDF PubMed Scopus (187) Google Scholar), this suggestion is consistent with the ability of 2-deoxyglucose to repress the stress-induced release of FGF1 and Myc-S100A13. Interestingly, unlike latrunculin (32Spector I. Schochet N.R. Blasberger D. Kashman Y. Cell Motil. Cytoskeleton. 1989; 13: 127-144Crossref PubMed Scopus (481) Google Scholar), amlexanox does not interfere with the stability of submembrane F-actin (16Landriscina M. Prudovsky I. Carreira C.M. Soldi R. Tarantini F. Maciag T. J. Biol. Chem. 2000; 275: 32753-32762Abstract Full Text Full Text PDF PubMed Scopus (36) Google Scholar), and this further implies that the F-actin stress fibers may be involved in the regulation of the transport of FGF1, p40 Syt1, and Myc-S100A13 in the nonclassical release of these polypeptides.The observation that S100A13 is constitutively released in vitro is also noteworthy, since a similar observation has been made with the intracellular p40 fragment of p65 Syt1 (8LaVallee T.M. Tarantini F. Gamble S. Carreira C.M. Jackson A. Maciag T. J. Biol. Chem. 1998; 273: 22217-22223Abstract Full Text Full Text PDF PubMed Scopus (67) Google Scholar). Interestingly, the function of the C2A domain in p40 Syt1 has been implicated in lipid bilayer penetration (51Chapman E.R. Davis A.F. J. Biol. Chem. 1998; 273: 4001-13995Abstract Full Text Full Text PDF PubMed Scopus (14) Google Scholar). However, unlike p40 Syt1, which exhibits constitutive release in FGF1 NIH 3T3 cell transfectants (8LaVallee T.M. Tarantini F. Gamble S. Carreira C.M. Jackson A. Maciag T. J. Biol. Chem. 1998; 273: 22217-22223Abstract Full Text Full Text PDF PubMed Scopus (67) Google Scholar), the expression of FGF1 in Myc-S100A13 NIH 3T3 cell transfectants represses the constitutive release of Myc-S100A13. Although it is difficult to interpret the significance of these data, it is possible that the ability of FGF1 to attenuate constitutive release of Myc-S100A13 but not the constitutive release of p40 Syt1 may reflect the ability of intracellular FGF1 to prefer an association with S100A13 rather than with p40 Syt1. Indeed, the observation that FGF1, S100A13, and p40 Syt1 are present as a noncovalent aggregate/complex in neural tissue suggests that the self-aggregration properties attributed to both the extravesicular p40 domain of p65 Syt1 (52Damer C.K. Creutz C.E. J. Neurochem. 1996; 67: 1661-1668Crossref PubMed Scopus (51) Google Scholar) and S100 gene family members (17Donato R. Biochim. Biophys. Acta. 1999; 1450: 191-231Crossref PubMed Scopus (592) Google Scholar, 18Heizmann C.W. Cox J.A. Biometals. 1998; 11: 383-397Crossref PubMed Scopus (259) Google Scholar) may be involved in the arrangement of a conformation-sensitive aggregate complex that may facilitate the release of FGF1. The observations that FGF1 (35Tarantini F. Gamble S. Jackson A. Maciag T. J. Biol. Chem. 1995; 270: 29039-29042Abstract Full Text Full Text PDF PubMed Scopus (59) Google Scholar), p40 Syt1 (53Marqueze B. Berton F. Seagar M. Biochimie ( Paris ). 2000; 82: 409-420Crossref PubMed Scopus (89) Google Scholar), and S100A13 (54Schafer B.W. Heizmann C.W. Trends Biochem. Sci. 1996; 21: 134-140Abstract Full Text PDF PubMed Scopus (1035) Google Scholar) are able to associate with acidic phospholipids further suggest an additional complexity to the stoichiometric interactions between these polypeptides.Although we do not know how this multiprotein aggregate/complex gains access to the extracellular compartment, it is likely that the basic residue-rich domain at the carboxyl terminus of S100A13 may be involved in regulating this function. Several studies have reported that the carboxyl-terminal domain of S100 proteins is involved in mediating the interaction of S100 polypeptides in their dimeric state with their target proteins (17Donato R. Biochim. Biophys. Acta. 1999; 1450: 191-231Crossref PubMed Scopus (592) Google Scholar, 18Heizmann C.W. Cox J.A. Biometals. 1998; 11: 383-397Crossref PubMed Scopus (259) Google Scholar). Because deletion of the basic residue-rich domain at the carboxyl terminus of Myc-S100A13 results in the generation of a dominant-negative effector of FGF1 release in response to temperature stress, it is likely that this domain may be involved in the regulation of FGF1 export under heat shock conditions. However, it is unlikely that the S100A13 basic residue-rich domain is involved in mediating the ability of Myc-S100A13 to traverse the plasma membrane, since the Myc-S100A13Δ88–98 mutant is released in response to heat shock. This is consistent with the observations that members of the S100 gene family lacking a basic residue-rich domain at their carboxyl terminus are released into the extracellular compartment following expression in mammalian cells (17Donato R. Biochim. Biophys. Acta. 1999; 1450: 191-231Crossref PubMed Scopus (592) Google Scholar, 18Heizmann C.W. Cox J.A. Biometals. 1998; 11: 383-397Crossref PubMed Scopus (259) Google Scholar, 21Rammes A. Roth J. Goebeler M. Klempt M. Hartmann M. Sorg C. J. Biol. Chem. 1997; 272: 9496-9502Abstract Full Text Full Text PDF PubMed Scopus (469) Google Scholar) and may imply that the carboxyl-terminal basic residue-rich domain in S100A13 functions to associate with target proteins, while the remainder of the S100A13 may be involved in penetration through the lipid bilayer. Indeed, S100B and S100A10 do not contain a basic residue-rich domain, yet S100B is released by glial cells (55Shashoua V.E. Hesse G.W. Moore B.W. J. Neurochem. 1984; 42: 1536-1541Crossref PubMed Scopus (138) Google Scholar, 56Van Eldik L.J. Zimmer D.B. Brain Res. 1987; 436: 367-370Crossref PubMed Scopus (148) Google Scholar), and S100A10 has been reported not only to associate with plasminogen in the extracellular compartment but is able to stimulate tissue-dependent plasminogen activation either alone or as a complex with Anx2 (57Kassam G. Le B.H. Choi K.S. Kang H.M. Fitzpatrick S.L. Louie P. Waisman D.M. Biochemistry. 1998; 37: 16958-16966Crossref PubMed Scopus (115) Google Scholar). These and other studies (5" @default.
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