Molecular interaction of neurocalcin alpha with alsin (ALS2).

Abstract:

:Membrane microdomains (MDs), or lipid rafts, are recently identified dynamic membrane domains on which various signal-transductions are performed. Intracellular Ca(2+)-binding proteins participate in the Ca(2+) signaling through interaction with various proteins. Neurocalcin alpha (NCalpha) is a member of neuronal calcium sensor (NCS) protein family and shows Ca(2+)-dependent binding to the cell membrane through N-terminal myristoyl moiety. Since NCalpha was identified as a Ca(2+)-dependent binding protein to neuronal MDs, its binding proteins may participate in the signal-transduction on the MDs. In an immunoprecipitate using anti-NCalpha antibody, alsin (ALS2), a protein product of one of the responsive genes for amyotrophic lateral sclerosis, was detected through LC-MS/MS. Specific antibody to alsin was produced and immunoprecipitation using this antibody showed co-sedimentation of NCalpha. Some part of alsin bound to brain-derived MD fraction in the presence of Ca(2+) ions and eluted out by the chelation of Ca(2+) ions, as in the case of NCalpha. Immunostaining of cultured neurons showed broad distribution of alsin and NCalpha, and membrane association of these proteins were increased through Ca(2+) loading by maitotoxin. These results suggest that alsin binds cell membrane in a Ca(2+)-dependent manner through NCalpha and regulates membrane dynamics.

journal_name

Neurosci Lett

journal_title

Neuroscience letters

authors

Masutani T,Taguchi K,Kumanogoh H,Nakamura S,Maekawa S

doi

10.1016/j.neulet.2008.04.066

subject

Has Abstract

pub_date

2008-06-13 00:00:00

pages

26-8

issue

1

eissn

0304-3940

issn

1872-7972

pii

S0304-3940(08)00537-5

journal_volume

438

pub_type

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