BAIT

VPS-35

CELE_F59G1.3, F59G1.3
related to yeast Vacuolar Protein Sorting factor
Caenorhabditis elegans
PREY

SNX-1

CELE_C05D9.1, vps-5, C05D9.1
snx-1 encodes a PX and BAR domain-containing protein that is the C. elegans ortholog of the Vps5/SNX1 subunit of the core retromer complex; in C. elegans, SNX-1 functions as a component of the retromer complex that, along with RME-8 and HSP-1, regulates retrograde endosome-to-Golgi transport through control of endosomal clathrin dynamics; SNX-1 binds RME-8 in vitro; SNX-1 is expressed in several different tissues, including the intestine, coelomocytes, and hypodermis; SNX-1 localizes to early endosomes, co-localizing with RME-8.
Caenorhabditis elegans

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Retromer is required for apoptotic cell clearance by phagocytic receptor recycling.

Chen D, Xiao H, Zhang K, Wang B, Gao Z, Jian Y, Qi X, Sun J, Miao L, Yang C

The cell surface receptor CED-1 mediates apoptotic cell recognition by phagocytic cells, enabling cell corpse clearance in Caenorhabditis elegans. Here, we found that the C. elegans intracellular protein sorting complex, retromer, was required for cell corpse clearance by mediating the recycling of CED-1. Retromer was recruited to the surfaces of phagosomes containing cell corpses, and its loss of function caused ... [more]

Science Mar. 05, 2010; 327(5970);1261-4 [Pubmed: 20133524]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
VPS-35 SNX-1
Co-fractionation
Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

High0.891BioGRID
2580688

Curated By

  • BioGRID