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Homeostatic tuning of Ca 2+ signal transduction by members of the calpacitin protein family
Author(s) -
Gerendasy Dan
Publication year - 1999
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/(sici)1097-4547(19991001)58:1<107::aid-jnr11>3.0.co;2-g
Subject(s) - signal transduction , homeostasis , signal (programming language) , microbiology and biotechnology , biology , neuroscience , chemistry , computer science , programming language
The calpacitin protein family is made up of small, abundantly expressed proteins that bind to the Ca 2+ ‐free form of calmodulin (CaM) with an affinity equal to or greater than that of the Ca 2+ ‐containing form. Their CaM‐binding domains are homologous and contain an IQ motif. Two members of this family, growth‐associated protein‐43 (GAP‐43) and RC3, have been implicated in long‐term potentiation (LTP) and the elaboration of pre‐ and postsynaptic structures. Computer‐aided modeling of calpacitin–CaM interactions suggests that these molecules regulate Ca 2+ flux size and CaM availability. Simulation of the interactions between the calpacitins CaM and Ca 2+ imply that GAP‐43 and RC3 tune and homeostatically constrain the Ca 2+ signal transduction system. In so doing, they link Ca 2+ fluxes to downstream elements of a signaling cascade that generates LTP. J. Neurosci. Res. 58:107–119, 1999. © 1999 Wiley‐Liss, Inc.