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Publication Abstract from PubMed

VAMP7 is involved in the fusion of late endocytic compartments with other membranes. One possible mechanism of VAMP7 delivery to these late compartments is via the AP3 trafficking adaptor. We show that the linker of the delta-adaptin subunit of AP3 binds the VAMP7 longin domain and determines the structure of their complex. Mutation of residues on both partners abolishes the interaction in vitro and in vivo. The binding of VAMP7 to delta-adaptin requires the VAMP7 SNARE motif to be engaged in SNARE complex formation and hence AP3 must transport VAMP7 when VAMP7 is part of a cis-SNARE complex. The absence of delta-adaptin causes destabilization of the AP3 complex in mouse mocha fibroblasts and mislocalization of VAMP7. The mislocalization can be rescued by transfection with wild-type delta-adaptin but not by delta-adaptin containing mutations that abolish VAMP7 binding, despite in all cases intact AP3 being present and LAMP1 trafficking being rescued.

Structural basis of the intracellular sorting of the SNARE VAMP7 by the AP3 adaptor complex.,Kent HM, Evans PR, Schafer IB, Gray SR, Sanderson CM, Luzio JP, Peden AA, Owen DJ Dev Cell. 2012 May 15;22(5):979-88. Epub 2012 Apr 19. PMID:22521722^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.