Structural requirements for VAP-B oligomerization and their implication in Als-associated VAP-B (P56S) neurotoxicity

We defined the structural requirements for VAP-B oligomerization and demonstrated their contribution for VAP-B(P56S) aggregation and neurotoxicity. We show that the oligomerization of VAP-B is mainly mediated by its coiled-coil domain, and that the GXXXG dimerization motif within the transmembrane domain (TMD) mediates TMDs self-association, but is insufficient to drive VAP-B oligomerization.

slid #6 From Sima Lev's presentation - VAP-B and its role in Amyotrophic lateral sclerosis
From Sima Lev’s presentation – VAP-B and its role in Amyotrophic lateral sclerosis

Sima Lev Web Team

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