Novel Syntaxin 6-Interacting Protein, SHIP164, Regulates Syntaxin 6-Dependent Sorting from Early Endosomes

Membrane fusion is dependent on the function of SNAREs and their α-helical SNARE motifs that form SNARE complexes. The Habc domains at the N-termini of some SNAREs can interact with their associated SNARE motif, Sec1/Munc18 (SM) proteins, tethering proteins or adaptor proteins, suggesting that they...

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Published in:Traffic (Copenhagen, Denmark) Denmark), 2010-05, Vol.11 (5), p.688-705
Main Authors: Otto, Grant P, Razi, Minoo, Morvan, Joëlle, Stenner, Frank, Tooze, Sharon A
Format: Article
Language:English
Subjects:
Amino Acid Motifs - genetics
Antigens, CD
Biological Transport - genetics
Endosomes - genetics
Endosomes - metabolism
GARP
Golgi Apparatus - genetics
Golgi Apparatus - metabolism
Humans
intracellular transport
KIAA0701
Mannosephosphates
Membrane Fusion - genetics
Protein Binding - genetics
Protein Structure, Secondary - genetics
Protein Structure, Tertiary - genetics
Protein Transport - genetics
Qa-SNARE Proteins - genetics
Qa-SNARE Proteins - metabolism
Receptor, IGF Type 2 - genetics
Receptor, IGF Type 2 - metabolism
Receptors, Transferrin - genetics
Receptors, Transferrin - metabolism
SNARE Proteins - genetics
SNARE Proteins - metabolism
SNAREs
trans Golgi network
Transport Vesicles - genetics
Transport Vesicles - metabolism
UHRF1BP1L
VFT
Vps13
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Summary:Membrane fusion is dependent on the function of SNAREs and their α-helical SNARE motifs that form SNARE complexes. The Habc domains at the N-termini of some SNAREs can interact with their associated SNARE motif, Sec1/Munc18 (SM) proteins, tethering proteins or adaptor proteins, suggesting that they play an important regulatory function. We screened for proteins that interact with the Habc domain of Syntaxin 6, and isolated an uncharacterized 164-kDa protein that we named SHIP164. SHIP164 is part of a large (~700 kDa) complex, and interacts with components of the Golgi-associated retrograde protein (GARP) tethering complex. Depletion of GARP subunits or overexpression of Syntaxin 6 results in a redistribution of soluble SHIP164 to endosomal structures. Co-overexpression of Syntaxin 6 and SHIP164 produced excessive tubulation of endosomes, and perturbed the transport of cation-independent mannose-6-phosphate receptor (CI-MPR) and transferrin receptor. Thus, we propose that SHIP164 functions in trafficking through the early/recycling endosomal system.
ISSN:1398-9219
1600-0854
DOI:10.1111/j.1600-0854.2010.01049.x