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Gene Review

VSNL1  -  visinin-like 1

Bos taurus

 
 
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High impact information on VSNL1

  • The predicted structure of CCaMK contains a catalytic domain followed by two regulatory domains, a calmodulin-binding domain and a visinin-like Ca(2+)-binding domain [1].
  • Moreover, repaglinide tightly bound to the visinin-like domain of CCaMK and PpCaMK in a Ca2+-dependent manner and antagonized the regulatory function of the domain with IC50 values of 55 and 4 microM for CCaMK and PpCaMK respectively [2].
  • In plants, lily CCaMK [chimaeric Ca2+/CaM (calmodulin)-dependent protein kinase] and its PpCaMK ( Physcomitrella patens CCaMK) homologue are characterized by a visinin-like domain with three EF-hands [2].
  • Although both repaglinide and a potent insulin secretagogue, namely glibenclamide, blocked K(ATP) channels with similar potency, glibenclamide had no antagonizing effect on the Ca2+-stimulated CCaMK and PpCaMK autophosphorylation, mediated by their visinin-like domain [2].
 

Biological context of VSNL1

  • The NCS (neuronal calcium sensor) proteins, including neurocalcins, recoverins and visinin-like proteins are members of a family of Ca2+-sensitive regulators, each with three Ca2+-binding EF-hand motifs [2].
 

Associations of VSNL1 with chemical compounds

References

  1. Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like calcium-binding domain. Patil, S., Takezawa, D., Poovaiah, B.W. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  2. Neuronal calcium sensor proteins are direct targets of the insulinotropic agent repaglinide. Okada, M., Takezawa, D., Tachibanaki, S., Kawamura, S., Tokumitsu, H., Kobayashi, R. Biochem. J. (2003) [Pubmed]
 
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