Extended synaptotagmin interaction with the fibroblast growth factor receptor depends on receptor conformation, not catalytic activity
| Autor: | Joëlle Baril, Sabrina Bellenfant, Tom Moss, Michel G. Tremblay, François Guillou, Prakash K. Mishra, Chelsea Herdman |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
endocrine system
animal structures Protein Conformation Molecular Sequence Data Tropomyosin receptor kinase B Biology Endoplasmic Reticulum Bioinformatics Tropomyosin receptor kinase C Biochemistry Synaptotagmins Growth factor receptor Catalytic Domain Enzyme-linked receptor Humans 5-HT5A receptor Amino Acid Sequence Receptor Fibroblast Growth Factor Type 1 Molecular Biology Insulin-like growth factor 1 receptor technology industry and agriculture Kinase insert domain receptor Cell Biology Cell biology nervous system ROR1 Additions and Corrections lipids (amino acids peptides and proteins) Sequence Alignment Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 291:3173 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.a115.656918 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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