Molecular Biology of the Cell Sign up for new MBC in Press e-TOCs!

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

Originally published as MBC in Press, 10.1091/mbc.E03-10-0777 on March 5, 2004

Vol. 15, Issue 5, 2218-2229, May 2004

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow MBC Videos
Right arrow All Versions of this Article:
E03-10-0777v1
15/5/2218    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Junutula, J. R.
Right arrow Articles by Scheller, R. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Junutula, J. R.
Right arrow Articles by Scheller, R. H.

Rab14 Is Involved in Membrane Trafficking between the Golgi Complex and Endosomes

Jagath R. Junutula * {dagger}, Ann M. De Maziére {dagger} {ddagger}, Andrew A. Peden *, Karen E. Ervin *, Raj J. Advani §, Suzanne M. van Dijk {ddagger}, Judith Klumperman {ddagger}, and Richard H. Scheller * ||

* Genentech Inc., South San Francisco, California 94080; {ddagger} Department of Cell Biology and Institute for Biomembranes, University Medical Center, 3584 CX Utrecht, The Netherlands; and § Department of Molecular and Cell Physiology, Beckman Center, Stanford University, Stanford, California 94305

Submitted October 31, 2003; Revised January 8, 2004; Accepted February 4, 2004
Monitoring Editor: David Botstein

Rab GTPases are localized to various intracellular compartments and are known to play important regulatory roles in membrane trafficking. Here, we report the subcellular distribution and function of Rab14. By immunofluorescence and immunoelectron microscopy, both endogenous as well as overexpressed Rab14 were localized to biosynthetic (rough endoplasmic reticulum, Golgi, and trans-Golgi network) and endosomal compartments (early endosomal vacuoles and associated vesicles). Notably overexpression of Rab14Q70L shifted the distribution toward the early endosome associated vesicles, whereas the S25N and N124I mutants induced a shift toward the Golgi region. A similar, although less pronounced, redistribution of the transferrin receptor was also observed in cells overexpressing Rab14 mutants. Impairment of Rab14 function did not however affect transferrin uptake or recycling kinetics. Together, these findings suggest that Rab14 is involved in the biosynthetic/recycling pathway between the Golgi and endosomal compartments.

Article published online ahead of print. Mol. Biol. Cell 10.1091/mbc.E03–10–0777. Article and publication date are available at www.molbiolcell.org/cgi/doi/10.1091/mbc.E03–10–0777.

Abbreviations used: EE, early endosome; EEA1, early endosomal antigen 1; GST, glutathione S-transferase; PNS, postnuclear supernatant; RE, recycling endosome; RER, rough endoplasmic reticulum; TfR, transferrin receptor; VTC, vesiculo-tubular cluster.

Online version of this article contains supporting material. Online version is available at www.molbiolcell.org.

{dagger} These authors contributed equally to this work.

|| Corresponding author. E-mail address: scheller{at}gene.com.




This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
D. K. Chun, J. M. McEwen, M. Burbea, and J. M. Kaplan
UNC-108/Rab2 Regulates Postendocytic Trafficking in Caenorhabditis elegans
Mol. Biol. Cell, July 1, 2008; 19(7): 2682 - 2695.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. Gou, A. Mishra, T. Weng, L. Su, N. R. Chintagari, Z. Wang, H. Zhang, L. Gao, P. Wang, H. M. Stricker, et al.
Annexin A2 Interactions with Rab14 in Alveolar Type II Cells
J. Biol. Chem., May 9, 2008; 283(19): 13156 - 13164.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
S. L. Schwartz, C. Cao, O. Pylypenko, A. Rak, and A. Wandinger-Ness
Rab GTPases at a glance
J. Cell Sci., November 15, 2007; 120(22): 3905 - 3910.
[Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
C. M. Babbey, N. Ahktar, E. Wang, C. C.-H. Chen, B. D. Grant, and K. W. Dunn
Rab10 Regulates Membrane Transport through Early Endosomes of Polarized Madin-Darby Canine Kidney Cells
Mol. Biol. Cell, July 1, 2006; 17(7): 3156 - 3175.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
J. G. Magadan, M. A. Barbieri, R. Mesa, P. D. Stahl, and L. S. Mayorga
Rab22a regulates the sorting of transferrin to recycling endosomes.
Mol. Cell. Biol., April 1, 2006; 26(7): 2595 - 2614.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
T. Baust, C. Czupalla, E. Krause, L. Bourel-Bonnet, and B. Hoflack
Proteomic analysis of adaptor protein 1A coats selectively assembled on liposomes
PNAS, February 28, 2006; 103(9): 3159 - 3164.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Larance, G. Ramm, J. Stockli, E. M. van Dam, S. Winata, V. Wasinger, F. Simpson, M. Graham, J. R. Junutula, M. Guilhaus, et al.
Characterization of the Role of the Rab GTPase-activating Protein AS160 in Insulin-regulated GLUT4 Trafficking
J. Biol. Chem., November 11, 2005; 280(45): 37803 - 37813.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. R. Junutula, E. Schonteich, G. M. Wilson, A. A. Peden, R. H. Scheller, and R. Prekeris
Molecular Characterization of Rab11 Interactions with Members of the Family of Rab11-interacting Proteins
J. Biol. Chem., August 6, 2004; 279(32): 33430 - 33437.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2004 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.