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XB-ART-50561
J Biol Chem June 26, 2015; 290 (26): 16142-56.
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Extended Synaptotagmin Interaction with the Fibroblast Growth Factor Receptor Depends on Receptor Conformation, Not Catalytic Activity.

Tremblay MG , Herdman C , Guillou F , Mishra PK , Baril J , Bellenfant S , Moss T .


Abstract
We previously demonstrated that ESyt2 interacts specifically with the activated FGF receptor and is required for a rapid phase of receptor internalization and for functional signaling via the ERK pathway in early Xenopus embryos. ESyt2 is one of the three-member family of Extended Synaptotagmins that were recently shown to be implicated in the formation of endoplasmic reticulum (ER)-plasma membrane (PM) junctions and in the Ca(2+) dependent regulation of these junctions. Here we show that ESyt2 is directed to the ER by its putative transmembrane domain, that the ESyts hetero- and homodimerize, and that ESyt2 homodimerization in vivo requires a TM adjacent sequence but not the SMP domain. ESyt2 and ESyt3, but not ESyt1, selectively interact in vivo with activated FGFR1. In the case of ESyt2, this interaction requires a short TM adjacent sequence and is independent of receptor autophosphorylation, but dependent on receptor conformation. The data show that ESyt2 recognizes a site in the upper kinase lobe of FGFR1 that is revealed by displacement of the kinase domain activation loop during receptor activation.

PubMed ID: 25922075
PMC ID: PMC4481215
Article link: J Biol Chem


Species referenced: Xenopus
Genes referenced: esyt1 esyt2 esyt3 fgfr1 mapk1

References [+] :
Andersen, How calcium makes endocytic receptors attractive. 2014, Pubmed