Targeting of calcium/calmodulin-dependent protein kinase II.

Content Provider	Semantic Scholar
Author	Colbran, Roger J.
Copyright Year	2004
Abstract	Calcium/calmodulin-dependent protein kinase II (CaMKII) has diverse roles in virtually all cell types and it is regulated by a plethora of mechanisms. Local changes in Ca2+ concentration drive calmodulin binding and CaMKII activation. Activity is controlled further by autophosphorylation at multiple sites, which can generate an autonomously active form of the kinase (Thr286) or can block Ca2+/calmodulin binding (Thr305/306). The regulated actions of protein phosphatases at these sites also modulate downstream signalling from CaMKII. In addition, CaMKII targeting to specific subcellular microdomains appears to be necessary to account for the known signalling specificity, and targeting is regulated by Ca2+/calmodulin and autophosphorylation. The present review focuses on recent studies revealing the diversity of CaMKII interactions with proteins localized to neuronal dendrites. Interactions with various subunits of the NMDA (N-methyl-D-aspartate) subtype of glutamate receptor have attracted the most attention, but binding of CaMKII to cytoskeletal and several other regulatory proteins has also been reported. Recent reports describing the molecular basis of each interaction and their potential role in the normal regulation of synaptic transmission and in pathological situations are discussed. These studies have revealed fundamental regulatory mechanisms that are probably important for controlling CaMKII functions in many cell types.
Starting Page	1
Ending Page	16
Page Count	16
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.biochemj.org/content/ppbiochemj/378/1/1.full.pdf
PubMed reference number	14653781v1
Volume Number	378
Part	1
Journal	The Biochemical journal
Language	English
Access Restriction	Open
Subject Keyword	Anatomical compartments Aspartic Acid Body tissue Calcium ion Calmodulin Catalytic Domain Cytoskeleton Dendrites Dimerization Glutamate Receptor Glutamic Acid Holoenzymes Manuscripts Multiprotein Complexes N-Methyl-D-Aspartate Receptors N-Methylaspartate Neurons Perilipins Phosphoric Monoester Hydrolases Protein Isoforms Protein Kinases Protein phosphatase Subgroup Synapses Synaptic Transmission biological signaling calmodulin-dependent protein kinase II cell type cellular targeting funding grant kinase activity subclass
Content Type	Text
Resource Type	Article