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PKC induces release of a functional ectodomain of the guidance cue semaphorin6A
Author(s) -
St. Clair Riley M.,
Dumas Caroline M.,
Williams Kori S.,
Goldstein Matthew T.,
Stant Elizabeth A.,
Ebert Alicia M.,
Ballif Bryan A.
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13561
Subject(s) - ectodomain , semaphorin , transmembrane protein , phosphorylation , microbiology and biotechnology , zebrafish , biology , transmembrane domain , signal transduction , kinase , protein kinase c , biochemistry , receptor , gene
Semaphorins (Semas) are a family of secreted and transmembrane proteins that play critical roles in development. Interestingly, several vertebrate transmembrane Sema classes are capable of producing functional soluble ectodomains. However, little is known of soluble Sema6 ectodomains in the nervous system. Herein, we show that the soluble Sema6A ectodomain, sS ema6A, exhibits natural and protein kinase C ( PKC )‐induced release. We show that PKC mediates Sema6A phosphorylation at specific sites and while this phosphorylation is not the primary mechanism regulating sS ema6A production, we found that the intracellular domain confers resistance to ectodomain release. Finally, sS ema6A is functional as it promotes the cohesion of zebrafish early eye field explants. This suggests that in addition to its canonical contact‐mediated functions, Sema6A may have regulated, long‐range, forward‐signaling capacity.