Journal
NATURE CELL BIOLOGY
Volume 7, Issue 9, Pages 887-U36Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb1290
Keywords
-
Categories
Ask authors/readers for more resources
Rab- family GTPases are conserved regulators of membrane trafficking that cycle between inactive GDP- bound and activated GTP- bound states(1,2). A key determinant of Rab function is the lifetime of the GTP- bound state(3). As Rabs have a low intrinsic rate of GTP hydrolysis, this process is under the control of GTP-hydrolysis-activating proteins ( GAPs) (1). Due to the large number of Rabs and GAPs that are encoded by the human genome, it has proven difficult to assign specific functional relationships to these proteins. Here, we identify a Rab5- specific GAP ( RabGAP5), and show that RN- Tre ( previously described as a Rab5 GAP) acts on Rab41. RabGAP- 5 overexpression triggers a loss of the Rab5 effector EEA1 from endosomes and blocks endocytic trafficking. By contrast, depletion of RabGAP- 5 results in increased endosome size, more endosome- associated EEA1, and disrupts the trafficking of EGF and LAMP1. RabGAP- 5 therefore limits the amount of activated Rab5, and thereby regulates trafficking through endosomes.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available