Differential Control of ErbB2 Surface Expression in Breast Cancer Cells by an Alternatively Spliced Form of ERBIN
Abstract
Receptor internalization following ligand stimulation is an important way of attenuating downstream signaling. One such family of proteins involved in this process are the Vps proteins. Vps proteins are a family of proteins first identified in Yeast that are required for proper vacuolar protein sorting (hence the name Vps). Yeast Snf7p is a small coiled-coiled protein involved in multivesicular body (MVB) function. Genomic and proteonomic studies indicate yeast Snf7p also interacts with Bro1-containing proteins, Bro1p and Rim20p, involved in MVB function and pH signal transduction, respectively. Here we report the identification of Snf7-1, one of a family of at least three human homologs of yeast Snf7p. Using affinity-capture experiments, we show that human Snf7-1 interacts with AIP1, a mammalian Bro1p-containing protein involved in apoptosis and cellular vacuolization. Snf7-1 did not, however, interact with another human Bro1-containing molecule, Rhophilin-2. Additional domain mapping using affinity-capture experiments revealed that the N-terminus of AIP1 was necessary and sufficient for interacting with Snf7-1. These results suggest the possibility that the Snf7-1-AIP1 interaction plays a role in mammalian MVB function.
Document Details
- Document Type
- Technical Report
- Publication Date
- May 01, 2003
- Accession Number
- ADA416779
Entities
People
- Jeremy W. Peck
Organizations
- Georgetown University