CASK stabilizes neurexin and links it to liprin-α in a neuronal activity-dependent manner

CASK stabilizes neurexin and links it to liprin-α in a neuronal activity-dependent manner CASK, a MAGUK family protein, is an essential protein present in the presynaptic compartment. CASK’s cellular role is unknown, but it interacts with multiple proteins important for synapse formation and function, including neurexin, liprin-α, and Mint1. CASK phosphorylates neurexin in a divalent ion-sensitive manner, although the functional relevance of this activity is unclear. Here we find that liprin-α and Mint1 compete for direct binding to CASK, but neurexin1β eliminates this competition, and all four proteins form a complex. We describe a novel mode of interaction between liprin-α and CASK when CASK is bound to neurexin1β. We show that CASK phosphorylates neurexin, modulating the interaction of liprin-α with the CASK–neurexin1β–Mint1 complex. Thus, CASK creates a regulatory and structural link between the presynaptic adhesion molecule neurexin and active zone organizer, liprin-α. In neuronal culture, CASK appears to regulate the stability of neurexin by linking it with this multi-protein presynaptic active zone complex. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Cellular and Molecular Life Sciences Springer Journals

CASK stabilizes neurexin and links it to liprin-α in a neuronal activity-dependent manner

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Publisher
Springer Journals
Copyright
Copyright © 2016 by Springer International Publishing
Subject
Life Sciences; Cell Biology; Biomedicine general; Life Sciences, general; Biochemistry, general
ISSN
1420-682X
eISSN
1420-9071
DOI
10.1007/s00018-016-2183-4
pmid
27015872
Publisher site
See Article on Publisher Site

Abstract

CASK, a MAGUK family protein, is an essential protein present in the presynaptic compartment. CASK’s cellular role is unknown, but it interacts with multiple proteins important for synapse formation and function, including neurexin, liprin-α, and Mint1. CASK phosphorylates neurexin in a divalent ion-sensitive manner, although the functional relevance of this activity is unclear. Here we find that liprin-α and Mint1 compete for direct binding to CASK, but neurexin1β eliminates this competition, and all four proteins form a complex. We describe a novel mode of interaction between liprin-α and CASK when CASK is bound to neurexin1β. We show that CASK phosphorylates neurexin, modulating the interaction of liprin-α with the CASK–neurexin1β–Mint1 complex. Thus, CASK creates a regulatory and structural link between the presynaptic adhesion molecule neurexin and active zone organizer, liprin-α. In neuronal culture, CASK appears to regulate the stability of neurexin by linking it with this multi-protein presynaptic active zone complex.

Journal

Cellular and Molecular Life SciencesSpringer Journals

Published: Mar 25, 2016

References

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