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Sez6l2 regulates phosphorylation of ADD and neuritogenesis.

Abstract：

:Increasing evidence shows that immune-mediated mechanisms may contribute to the pathogenesis of central nervous system disorders including cerebellar ataxias, as indicated by the aberrant production of neuronal surface antibodies. We previously reported a patient with cerebellar ataxia associated with production of a new anti-neuronal antibody, anti-seizure-related 6 homolog like 2 (Sez6l2). Sez6l2 is a type 1 membrane protein that is highly expressed in the hippocampus and cerebellar cortex and mice lacking Sez6l2 protein family members develop ataxia. Here we used a proteomics-based approach to show that serum derived from this patient recognizes the extracellular domain of Sez6l2 and that Sez6l2 protein binds to both adducin (ADD) and glutamate receptor 1 (GluR1). Our results indicate that Sez6l2 is one of the auxiliary subunits of the AMPA receptor and acts as a scaffolding protein to link GluR1 to ADD. Furthermore, Sez6l2 overexpression upregulates ADD phosphorylation, whereas siRNA-mediated downregulation of Sez612 prevents ADD phosphorylation, suggesting that Sez6l2 modulates AMPA-ADD signal transduction.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Yaguchi H,Yabe I,Takahashi H,Watanabe M,Nomura T,Kano T,Matsumoto M,Nakayama KI,Watanabe M,Hatakeyama S

doi

10.1016/j.bbrc.2017.10.047

subject

Has Abstract

pub_date

2017-12-09 00:00:00

pages

234-241

issue

1-2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(17)32017-X

journal_volume

494

pub_type

杂志文章

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