JCB logo
PeproTech: Your source for Cell Biology Research Reagents
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online November 26, 2007
doi:10.1083/jcb.200702187
The Journal of Cell Biology, Vol. 179, No. 5, 965-980
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Shah et al.
This Article
Right arrow Full Text
Right arrow PDF (Full Text)
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Shah, A. H.
Right arrow Articles by Carlin, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shah, A. H.
Right arrow Articles by Carlin, C.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Article

 Adenovirus RID{alpha} regulates endosome maturation by mimicking GTP-Rab7

Ankur H. Shah1,2, Nicholas L. Cianciola1, Jeffrey L. Mills1, Frank D. Sönnichsen1, and Cathleen Carlin1,2,3

1 Department of Physiology and Biophysics, 2 Molecular Virology Training Program, and 3 Case Comprehensive Cancer Center, School of Medicine, Case Western Reserve University, Cleveland, OH 44106

Correspondence to Cathleen Carlin: cathleen.carlin{at}case.edu

The small guanosine triphosphatase Rab7 regulates late endocytic trafficking. Rab7-interacting lysosomal protein (RILP) and oxysterol-binding protein–related protein 1L (ORP1L) are guanosine triphosphate (GTP)–Rab7 effectors that instigate minus end–directed microtubule transport. We demonstrate that RILP and ORP1L both interact with the group C adenovirus protein known as receptor internalization and degradation {alpha} (RID{alpha}), which was previously shown to clear the cell surface of several membrane proteins, including the epidermal growth factor receptor and Fas (Carlin, C.R., A.E. Tollefson, H.A. Brady, B.L. Hoffman, and W.S. Wold. 1989. Cell. 57:135–144; Shisler, J., C. Yang, B. Walter, C.F. Ware, and L.R. Gooding. 1997. J. Virol. 71:8299–8306). RID{alpha} localizes to endocytic vesicles but is not homologous to Rab7 and is not catalytically active. We show that RID{alpha} compensates for reduced Rab7 or dominant-negative (DN) Rab7(T22N) expression. In vitro, Cu2+ binding to RID{alpha} residues His75 and His76 facilitates the RILP interaction. Site-directed mutagenesis of these His residues results in the loss of RID{alpha}–RILP interaction and RID{alpha} activity in cells. Additionally, expression of the RILP DN C-terminal region hinders RID{alpha} activity during an acute adenovirus infection. We conclude that RID{alpha} coordinates recruitment of these GTP-Rab7 effectors to compartments that would ordinarily be perceived as early endosomes, thereby promoting the degradation of selected cargo.

Abbreviations used in this paper: ANOVA, analysis of variance; DN, dominant negative; E3, early region 3; EGFR, EGF receptor; Hsp, heat-shock protein; LDL, low-density lipoprotein; MTOC, microtubule organizing center; MVB, multivesicular body; NMR, nuclear magnetic resonance; ORP, oxysterol-binding protein–related protein; RID, receptor internalization and degradation; RILP, Rab7-interacting lysosomal protein; TNFR1, TNF receptor 1; TRAIL-R, TNF-related apoptosis-inducing ligand receptor.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?




  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents