Matches in SemOpenAlex for { <https://semopenalex.org/work/W2024149807> ?p ?o ?g. }
- W2024149807 endingPage "15249" @default.
- W2024149807 startingPage "15242" @default.
- W2024149807 abstract "In a recent study (Goltz, J. S., Wolkoff, A. W., Novikoff, P. M., Stockert, R. J., and Satir, P.(1992) Proc. Natl. Acad. Sci. U. S. A. 89, 7026-7030), we found that ligand- and receptor-containing endocytic vesicles bind to endogenous microtubules in vitro after 60 min of receptor-mediated endocytosis of asialo-orosomucoid. In the presence of ATP, ligand-containing endocytic vesicles are released from microtubules, while those containing receptor are not. We hypothesized that cytoplasmic dynein may associate with ligand-containing, but not receptor-containing, domains of endocytic vesicles and might be involved in the movement of ligand-containing vesicles along microtubules during sorting of ligand from receptor. Direct evidence in support of this hypothesis has been obtained in the present study. Binding of ligand-containing vesicles to microtubules correlates highly (p < 0.001) with binding of dynein, but not kinesin, under a variety of conditions. Binding of receptor-containing vesicles to microtubules is independent of both cytoplasmic dynein and kinesin binding. Tight association of cytoplasmic dynein with a population of ligand-containing vesicles is seen directly by immunoprecipitation. These results support the view that in receptor-mediated endocytosis, ligand-containing vesicles become bound to microtubules by cytoplasmic dynein. While receptor domains of endosomes remain attached to microtubules in an ATP-independent manner, ligand-containing domains might be moved away toward pericentrosomal lysosomes by this motor molecule. In a recent study (Goltz, J. S., Wolkoff, A. W., Novikoff, P. M., Stockert, R. J., and Satir, P.(1992) Proc. Natl. Acad. Sci. U. S. A. 89, 7026-7030), we found that ligand- and receptor-containing endocytic vesicles bind to endogenous microtubules in vitro after 60 min of receptor-mediated endocytosis of asialo-orosomucoid. In the presence of ATP, ligand-containing endocytic vesicles are released from microtubules, while those containing receptor are not. We hypothesized that cytoplasmic dynein may associate with ligand-containing, but not receptor-containing, domains of endocytic vesicles and might be involved in the movement of ligand-containing vesicles along microtubules during sorting of ligand from receptor. Direct evidence in support of this hypothesis has been obtained in the present study. Binding of ligand-containing vesicles to microtubules correlates highly (p < 0.001) with binding of dynein, but not kinesin, under a variety of conditions. Binding of receptor-containing vesicles to microtubules is independent of both cytoplasmic dynein and kinesin binding. Tight association of cytoplasmic dynein with a population of ligand-containing vesicles is seen directly by immunoprecipitation. These results support the view that in receptor-mediated endocytosis, ligand-containing vesicles become bound to microtubules by cytoplasmic dynein. While receptor domains of endosomes remain attached to microtubules in an ATP-independent manner, ligand-containing domains might be moved away toward pericentrosomal lysosomes by this motor molecule." @default.
- W2024149807 created "2016-06-24" @default.
- W2024149807 creator A5006629649 @default.
- W2024149807 creator A5008681401 @default.
- W2024149807 creator A5016226507 @default.
- W2024149807 creator A5031545157 @default.
- W2024149807 creator A5085107070 @default.
- W2024149807 creator A5086039311 @default.
- W2024149807 creator A5091083651 @default.
- W2024149807 date "1995-06-01" @default.
- W2024149807 modified "2023-10-17" @default.
- W2024149807 title "Interaction of the Microtubule Cytoskeleton with Endocytic Vesicles and Cytoplasmic Dynein in Cultured Rat Hepatocytes" @default.
- W2024149807 cites W1508340724 @default.
- W2024149807 cites W1574829574 @default.
- W2024149807 cites W1775749144 @default.
- W2024149807 cites W1908837652 @default.
- W2024149807 cites W1965675171 @default.
- W2024149807 cites W1966298372 @default.
- W2024149807 cites W1966401796 @default.
- W2024149807 cites W1968535181 @default.
- W2024149807 cites W1980851644 @default.
- W2024149807 cites W1982275607 @default.
- W2024149807 cites W1986677906 @default.
- W2024149807 cites W1990276386 @default.
- W2024149807 cites W1993762028 @default.
- W2024149807 cites W2006666141 @default.
- W2024149807 cites W2013664403 @default.
- W2024149807 cites W2015229379 @default.
- W2024149807 cites W2016894006 @default.
- W2024149807 cites W2023150579 @default.
- W2024149807 cites W2025483718 @default.
- W2024149807 cites W2030808309 @default.
- W2024149807 cites W2033644851 @default.
- W2024149807 cites W2039273064 @default.
- W2024149807 cites W2040000700 @default.
- W2024149807 cites W2047307597 @default.
- W2024149807 cites W2048464939 @default.
- W2024149807 cites W2050905943 @default.
- W2024149807 cites W2057963096 @default.
- W2024149807 cites W2057975341 @default.
- W2024149807 cites W2059956955 @default.
- W2024149807 cites W2060803650 @default.
- W2024149807 cites W2065227756 @default.
- W2024149807 cites W2073764400 @default.
- W2024149807 cites W2075632813 @default.
- W2024149807 cites W2076826295 @default.
- W2024149807 cites W2078724694 @default.
- W2024149807 cites W2081406767 @default.
- W2024149807 cites W2082631326 @default.
- W2024149807 cites W2103138603 @default.
- W2024149807 cites W2118642774 @default.
- W2024149807 cites W2127012355 @default.
- W2024149807 cites W2133771191 @default.
- W2024149807 cites W2163898551 @default.
- W2024149807 cites W2175128997 @default.
- W2024149807 cites W2178522090 @default.
- W2024149807 cites W2395246509 @default.
- W2024149807 cites W2404271745 @default.
- W2024149807 doi "https://doi.org/10.1074/jbc.270.25.15242" @default.
- W2024149807 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7797509" @default.
- W2024149807 hasPublicationYear "1995" @default.
- W2024149807 type Work @default.
- W2024149807 sameAs 2024149807 @default.
- W2024149807 citedByCount "78" @default.
- W2024149807 countsByYear W20241498072013 @default.
- W2024149807 countsByYear W20241498072014 @default.
- W2024149807 countsByYear W20241498072015 @default.
- W2024149807 countsByYear W20241498072016 @default.
- W2024149807 countsByYear W20241498072017 @default.
- W2024149807 countsByYear W20241498072020 @default.
- W2024149807 crossrefType "journal-article" @default.
- W2024149807 hasAuthorship W2024149807A5006629649 @default.
- W2024149807 hasAuthorship W2024149807A5008681401 @default.
- W2024149807 hasAuthorship W2024149807A5016226507 @default.
- W2024149807 hasAuthorship W2024149807A5031545157 @default.
- W2024149807 hasAuthorship W2024149807A5085107070 @default.
- W2024149807 hasAuthorship W2024149807A5086039311 @default.
- W2024149807 hasAuthorship W2024149807A5091083651 @default.
- W2024149807 hasBestOaLocation W20241498071 @default.
- W2024149807 hasConcept C102747710 @default.
- W2024149807 hasConcept C106987784 @default.
- W2024149807 hasConcept C116569031 @default.
- W2024149807 hasConcept C130316041 @default.
- W2024149807 hasConcept C134729014 @default.
- W2024149807 hasConcept C170493617 @default.
- W2024149807 hasConcept C190062978 @default.
- W2024149807 hasConcept C20418707 @default.
- W2024149807 hasConcept C28005876 @default.
- W2024149807 hasConcept C41625074 @default.
- W2024149807 hasConcept C55493867 @default.
- W2024149807 hasConcept C59006786 @default.
- W2024149807 hasConcept C79747257 @default.
- W2024149807 hasConcept C86803240 @default.
- W2024149807 hasConcept C95444343 @default.
- W2024149807 hasConceptScore W2024149807C102747710 @default.
- W2024149807 hasConceptScore W2024149807C106987784 @default.
- W2024149807 hasConceptScore W2024149807C116569031 @default.
- W2024149807 hasConceptScore W2024149807C130316041 @default.