mVps24p functions in EGF receptor sorting/trafficking from the early endosome

Exp Cell Res. 2005 Mar 10;304(1):265-73. doi: 10.1016/j.yexcr.2004.11.003.

Qing Yan ¹, Piper Reid Hunt, Laurence Frelin, Thomas A Vida, Jonathan Pevsner, Andrew J Bean

Affiliations

Affiliation

1 Department of Neurobiology and Anatomy, The University of Texas Medical School at Houston, 6431 Fannin Street, MSB 7.007, Houston, TX 77030, USA.

PMID: 15707591 DOI: 10.1016/j.yexcr.2004.11.003

Abstract

Yeast Vps24p (vacuolar protein sorting) is part of a protein complex suggested to function in sorting/trafficking during endocytosis. We have characterized a mammalian homolog of the yeast protein, mVps24p, and examined its role in epidermal growth factor receptor trafficking. Endogenous mVps24p was distributed in both cytosol and in puncta and partially colocalized with markers for the trans-Golgi network. Adventitious expression of hrs or a mVps4p mutant deficient in ATPase activity caused a redistribution of both mVps24p and the M6PR to the resultant clustered/enlarged early endosomes. Expression of an mVps24p N-terminal fragment, that interacts with phosphatidylinositol 3,5-bisphosphate but not with mVps4p, produces enlarged early endosomes. More importantly, the mVps24p N-terminal fragment resulted in not only enhanced recycling, but also decreased degradation of the EGF receptor. These findings are consistent with a model in which mVps24p has a role in trafficking from the early endosome.

Name
Email *

	Sorry, but the email address you supplied was invalid.