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The J-domain protein Rme-8 interacts with Hsc70 to control clathrin-dependent endocytosis in Drosophila

The J-domain protein Rme-8 interacts with Hsc70 to control clathrin-dependent endocytosis in... By screening for mutants exhibiting interactions with a dominant-negative dynamin, we have identified the Drosophila homologue of receptor-mediated endocytosis (Rme) 8, a J-domain–containing protein previously shown to be required for endocytosis in Caenorhabditis elegans . Analysis of Drosophila Rme-8 mutants showed that internalization of Bride of sevenless and the uptake of tracers were blocked. In addition, endosomal organization and the distribution of clathrin were greatly disrupted in Rme-8 cells, suggesting that Rme-8 participates in a clathrin-dependent process. The phenotypes of Rme-8 mutants bear a strong resemblance to those of Hsc70-4 , suggesting that these two genes act in a common pathway. Indeed, biochemical and genetic data demonstrated that Rme-8 interacts specifically with Hsc70-4 via its J-domain. Thus, Rme-8 appears to function as an unexpected but critical cochaperone with Hsc70 in endocytosis. Because Hsc70 is known to act in clathrin uncoating along with auxilin, another J-protein, its interaction with Rme-8 indicates that Hsc70 can act with multiple cofactors, possibly explaining its pleiotropic effects on the endocytic pathway. endocytosis; clathrin; Hsc70; Rme-8; J-domain Footnotes The online version of this article includes supplemental material. Abbreviations used in this paper: Boss, Bride of sevenless; CCV, clathrin-coated vesicle; Clc, clathrin light chain; Hk, Hook; Rme, receptor-mediated endocytosis; shi , shibire ; TR-avidin, Texas red–conjugated avidin. Submitted: 17 November 2003 Accepted: 17 February 2004 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Cell Biology Rockefeller University Press

The J-domain protein Rme-8 interacts with Hsc70 to control clathrin-dependent endocytosis in Drosophila

Chang, Henry C.; Hull, Michael; Mellman, Ira
The Journal of Cell Biology , Volume 164 (7): 1055 – Mar 29, 2004
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References (58)

Publisher
Rockefeller University Press
Copyright
© 2004 Rockefeller University Press
ISSN
0021-9525
eISSN
1540-8140
DOI
10.1083/jcb.200311084
pmid
15051737
Publisher site
See Article on Publisher Site

Abstract

By screening for mutants exhibiting interactions with a dominant-negative dynamin, we have identified the Drosophila homologue of receptor-mediated endocytosis (Rme) 8, a J-domain–containing protein previously shown to be required for endocytosis in Caenorhabditis elegans . Analysis of Drosophila Rme-8 mutants showed that internalization of Bride of sevenless and the uptake of tracers were blocked. In addition, endosomal organization and the distribution of clathrin were greatly disrupted in Rme-8 cells, suggesting that Rme-8 participates in a clathrin-dependent process. The phenotypes of Rme-8 mutants bear a strong resemblance to those of Hsc70-4 , suggesting that these two genes act in a common pathway. Indeed, biochemical and genetic data demonstrated that Rme-8 interacts specifically with Hsc70-4 via its J-domain. Thus, Rme-8 appears to function as an unexpected but critical cochaperone with Hsc70 in endocytosis. Because Hsc70 is known to act in clathrin uncoating along with auxilin, another J-protein, its interaction with Rme-8 indicates that Hsc70 can act with multiple cofactors, possibly explaining its pleiotropic effects on the endocytic pathway. endocytosis; clathrin; Hsc70; Rme-8; J-domain Footnotes The online version of this article includes supplemental material. Abbreviations used in this paper: Boss, Bride of sevenless; CCV, clathrin-coated vesicle; Clc, clathrin light chain; Hk, Hook; Rme, receptor-mediated endocytosis; shi , shibire ; TR-avidin, Texas red–conjugated avidin. Submitted: 17 November 2003 Accepted: 17 February 2004

Journal

The Journal of Cell Biology – Rockefeller University Press

Published: Mar 29, 2004

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