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• W1987719880 abstract "A recent study shows that contacts between the endoplasmic reticulum and mitochondria occur preferentially on acetylated microtubules, providing physiological support for the microtubule track selectivity of molecular motors. A recent study shows that contacts between the endoplasmic reticulum and mitochondria occur preferentially on acetylated microtubules, providing physiological support for the microtubule track selectivity of molecular motors. Microtubules play a great variety of roles in the eukaryotic cell. Foremost, in interphase cells, microtubules act as the tracks upon which molecular motors traverse as they distribute myriad cellular cargoes throughout the cytoplasm. This microtubule-based transport is essential for any cell to establish the polarity and asymmetry necessary for its function. The αβ-tubulin heterodimer, the building block of microtubules, is subject to numerous reversible post-translational modifications. These modifications include acetylation at lysine 40 of α-tubulin, and detyrosination, palmitoylation, phosphorylation, polyglutamylation, and polyglycylation of the carboxy-terminal tail of both α and β tubulins [1Westermann S. Weber K. Post-translational modifications regulate microtubule function.Nat. Rev. Mol. Cell Biol. 2003; 4: 938-947Crossref PubMed Scopus (546) Google Scholar]. Microscopically, all microtubules look identical. However, their post-translational modifications, in combination with the presence of multiple isoforms of tubulin itself, create a variety of microtubules that may be differentially recognized by molecular motors or other proteins that bind microtubules. Until recently, though, there has been little indication that these modifications are of physiological significance. Experimental evidence is mounting to suggest that kinesin-1 preferentially binds to and moves along stable microtubules modified by polyglutamylation, acetylation, or detyrosination [2Liao G. Gundersen G.G. Kinesin is a candidate for cross-bridging microtubules and intermediate filaments. Selective binding of kinesin to detyrosinated tubulin and vimentin.J. Biol. Chem. 1998; 273: 9797-9803Crossref PubMed Scopus (223) Google Scholar, 3Reed N.A. Cai D. Blasius T.L. Jih G.T. Meyhofer E. Gaertig J. Verhey K.J. Microtubule acetylation promotes kinesin-1 binding and transport.Curr. Biol. 2006; 16: 2166-2172Abstract Full Text Full Text PDF PubMed Scopus (616) Google Scholar, 4Dompierre J.P. Godin J.D. Charrin B.C. Cordelieres F.P. King S.J. Humbert S. Saudou F. Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation.J. Neurosci. 2007; 27: 3571-3583Crossref PubMed Scopus (544) Google Scholar, 5Konishi Y. Setou M. Tubulin tyrosination navigates the kinesin-1 motor domain to axons.Nat. Neurosci. 2009; 12: 559-567Crossref PubMed Scopus (262) Google Scholar, 6Cai D. McEwen D.P. Martens J.R. Meyhofer E. Verhey K.J. Single molecule imaging reveals differences in microtubule track selection between Kinesin motors.PLoS Biol. 2009; 7: e1000216Crossref PubMed Scopus (189) Google Scholar, 7Hammond J.W. Huang C.F. Kaech S. Jacobson C. Banker G. Verhey K.J. Posttranslational modifications of tubulin and the polarized transport of kinesin-1 in neurons.Mol. Biol. Cell. 2010; 21: 572-583Crossref PubMed Scopus (184) Google Scholar]. Although the molecular basis for the differential binding of kinesin-1 to modified microtubules is not yet understood, it may be an important part of the mechanism underlying the selective distribution of cargoes along particular microtubule tracks. A recent study by Friedman et al. [8Friedman J.R. Webster B.M. Mastronarde D.N. Verhey K.J. Voeltz G.K. ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules.J. Cell Biol. 2010; 190: 363-375Crossref PubMed Scopus (232) Google Scholar] now shows that the distributions of two kinesin-1 cargoes — the endoplasmic reticulum (ER) and mitochondria — are influenced by microtubule acetylation. These new data provide a functional framework in which to view the importance of microtubule modifications. The ER forms an extensive and dynamic network in eukaryotic cells, one that is constantly reorganizing. Rearrangements of the network involve growth and shrinkage of ER tubules, fusion between tubules, and movement of tubules and sheets. Movements of these ER structures are important in many cellular functions in which contact with other membranes is required [9Voeltz G.K. Rolls M.M. Rapoport T.A. Structural organization of the endoplasmic reticulum.EMBO Rep. 2002; 3: 944-950Crossref PubMed Scopus (352) Google Scholar]. The ER is closely associated with the microtubule network [10Terasaki M. Chen L.B. Fujiwara K. Microtubules and the endoplasmic reticulum are highly interdependent structures.J. Cell Biol. 1986; 103: 1557-1568Crossref PubMed Scopus (442) Google Scholar], and its reorganization is achieved via two microtubule-dependent mechanisms. In the first mechanism, the growing microtubule tip drives rearrangement of the ER network through the tip attachment complex. ER tubules attach to the growing ends of dynamic microtubules and grow or shrink along with the microtubules. As this mechanism depends on the polymerization of microtubules, treating cells with microtubule-stabilizing or -depolymerizing agents, such as nocodazole, inhibits the ER movements mediated by the tip attachment complex [11Waterman-Storer C.M. Salmon E.D. Endoplasmic reticulum membrane tubules are distributed by microtubules in living cells using three distinct mechanisms.Curr. Biol. 1998; 8: 798-806Abstract Full Text Full Text PDF PubMed Google Scholar]. The second and more common mechanism of ER reorganization, called ER sliding, involves extension of ER tubules along the length of microtubules [12Allan V. Vale R. Movement of membrane tubules along microtubules in vitro: evidence for specialised sites of motor attachment.J. Cell Sci. 1994; 107: 1885-1897PubMed Google Scholar]. This mechanism is not dependent on microtubule dynamics, but is thought to occur via the action of the molecular motors kinesin-1 and cytoplasmic dynein [13Wozniak M.J. Bola B. Brownhill K. Yang Y.C. Levakova V. Allan V.J. Role of kinesin-1 and cytoplasmic dynein in endoplasmic reticulum movement in VERO cells. J.Cell Sci. 2009; 122: 1979-1989Crossref PubMed Scopus (96) Google Scholar]. Friedman et al. [8Friedman J.R. Webster B.M. Mastronarde D.N. Verhey K.J. Voeltz G.K. ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules.J. Cell Biol. 2010; 190: 363-375Crossref PubMed Scopus (232) Google Scholar] set out to examine the differences in ER dynamics between these two mechanisms in order to better understand how each mode of ER motility might contribute to particular functions of the ER. The authors found that, upon prolonged nocodazole treatment of COS-7 cells, ER movements were not completely abolished. Immunostaining revealed a population of nocodazole-resistant microtubules that were highly acetylated; thus, the authors began to investigate the relationship between ER movements and microtubule acetylation. ER sliding events were found to occur more frequently on microtubules that were acetylated than on those that were not. Further, the authors demonstrated that treating cells with drugs to inhibit deacetylase activity, thereby increasing microtubule acetylation, led to more frequent ER sliding events. These observations suggest that acetylation promotes ER motility, although the authors did not directly determine whether acetylation affects the stability of microtubules, per se, or whether an increase in stability may also influence movements of the ER. These data are consistent with results from two other groups [3Reed N.A. Cai D. Blasius T.L. Jih G.T. Meyhofer E. Gaertig J. Verhey K.J. Microtubule acetylation promotes kinesin-1 binding and transport.Curr. Biol. 2006; 16: 2166-2172Abstract Full Text Full Text PDF PubMed Scopus (616) Google Scholar, 4Dompierre J.P. Godin J.D. Charrin B.C. Cordelieres F.P. King S.J. Humbert S. Saudou F. Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation.J. Neurosci. 2007; 27: 3571-3583Crossref PubMed Scopus (544) Google Scholar], which showed that microtubule acetylation promotes binding and movement of kinesin-1 both in vitro and in vivo. Interestingly, the site of tubulin acetylation (lysine 40) is located in the lumen of the microtubule [14Nogales E. Whittaker M. Milligan R.A. Downing K.H. High-resolution model of the microtubule.Cell. 1999; 96: 79-88Abstract Full Text Full Text PDF PubMed Scopus (939) Google Scholar]; it is therefore not directly accessible to microtubule-binding proteins. It is more likely, then, that acetylation slightly alters the structure of the microtubule to promote selective binding. Furthermore, as acetylation occurs only after microtubule polymerization, the enzyme responsible for this modification should probably localize to the microtubule lumen. The preference of ER sliding for acetylated microtubules may indicate a functional difference between this type of ER motility and that mediated by the tip attachment complex. Intermembrane contacts are important for many functions of the ER and other membranous compartments [9Voeltz G.K. Rolls M.M. Rapoport T.A. Structural organization of the endoplasmic reticulum.EMBO Rep. 2002; 3: 944-950Crossref PubMed Scopus (352) Google Scholar]. The authors' results led them to hypothesize that the sliding mechanism may be used as a way for ER tubules to find and contact other organelles along a subpopulation of microtubules. To explore this possibility, Friedman et al. [8Friedman J.R. Webster B.M. Mastronarde D.N. Verhey K.J. Voeltz G.K. ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules.J. Cell Biol. 2010; 190: 363-375Crossref PubMed Scopus (232) Google Scholar] tracked the movements of two other organelles, mitochondria and endosomes, with respect to both ER and acetylated microtubules. A majority of both organelles remained in persistent contact with the ER. However, only mitochondria appeared to also localize preferentially to acetylated microtubules, suggesting that ER contacts with mitochondria, but not endosomes, are enriched along acetylated microtubules. Consistent with this finding is the fact that both ER and mitochondria are cargoes of kinesin-1, while endosomes are moved by KIF16B, a member of the kinesin-3 family [15Hoepfner S. Severin F. Cabezas A. Habermann B. Runge A. Gillooly D. Stenmark H. Zerial M. Modulation of receptor recycling and degradation by the endosomal kinesin KIF16B.Cell. 2005; 121: 437-450Abstract Full Text Full Text PDF PubMed Scopus (239) Google Scholar]. Further, work by Cai et al. [6Cai D. McEwen D.P. Martens J.R. Meyhofer E. Verhey K.J. Single molecule imaging reveals differences in microtubule track selection between Kinesin motors.PLoS Biol. 2009; 7: e1000216Crossref PubMed Scopus (189) Google Scholar] showed that another kinesin-3 family member, KIF1A, displayed no preference for acetylated microtubules in COS-7 cells. By biasing protein association with a particular subset of microtubules, acetylation allows for subpopulations of microtubules to act as compartments along which specific cargoes can find each other, and be found in return. In a sense, these microtubule compartments can be thought of as cellular pubs that attract a specific cargo crowd for mingling. Microtubule acetylation is also probably involved in the regulation of cell migration both in fibroblasts [16Gundersen G.G. Bulinski J.C. Selective stabilization of microtubules oriented toward the direction of cell migration.Proc. Natl. Acad. Sci. USA. 1988; 85: 5946-5950Crossref PubMed Scopus (212) Google Scholar] and neurons [17Creppe C. Malinouskaya L. Volvert M.L. Gillard M. Close P. Malaise O. Laguesse S. Cornez I. Rahmouni S. Ormenese S. et al.Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin.Cell. 2009; 136: 551-564Abstract Full Text Full Text PDF PubMed Scopus (354) Google Scholar]. It is attractive to speculate that polarization of moving cells requires kinesin-dependent recruitment of selective cargoes to the leading edge of migrating cells. Additional investigation is necessary to determine whether this selective motor recruitment applies to other microtubule modifications and other motor proteins. It is possible that at least some other microtubule motors have a higher affinity for either a specific tubulin isoform or a particular post-translational modification, similar to the preferential recruitment of kinesin-1 to acetylated microtubules. Such selectivity could create multiple microtubule compartments to recruit particular cargoes — different pubs for different crowds (Figure 1). Once bound to microtubules, the cargo can undergo bidirectional transport to facilitate its movement through the crowded cytoplasm. Cargoes recruited to the same subset of microtubules will interact with much higher efficiency, thus promoting exchange of molecules between particular cell compartments. If this simple model is correct, it indicates that, in addition to their role as tracks for long-distance transport, microtubules serve an important role as scaffolds for the organization and compartmentalization of the otherwise randomly distributed cellular components." @default.
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• W1987719880 title "Intracellular Transport: ER and Mitochondria Meet and Greet along Designated Tracks" @default.
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