CaMKII - Revision history

Avertyshev@mail.ru: /* Structure */

2019-04-16T13:08:27Z

‎Structure

Avertyshev@mail.ru at 13:07, 16 April 2019

2019-04-16T13:07:15Z

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Avertyshev@mail.ru at 09:56, 11 April 2019

2019-04-11T09:56:00Z

Avertyshev@mail.ru at 15:56, 10 April 2019

2019-04-10T15:56:23Z

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Avertyshev@mail.ru: Created page with "CaMKII. Calcium/Calmodulin Dependent Protein Kinase II. Ver. 0.3. This calcium calmodulin-dependent protein kinase is composed of four different chains: alpha, beta, gamma,..."

2019-04-09T09:58:47Z

Created page with "CaMKII. Calcium/Calmodulin Dependent Protein Kinase II. Ver. 0.3. This calcium calmodulin-dependent protein kinase is composed of four different chains: alpha, beta, gamma,..."

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CaMKII. Calcium/Calmodulin Dependent Protein Kinase II. Ver. 0.3.

This calcium calmodulin-dependent protein kinase is composed of four different chains: alpha, beta, gamma, and delta. An enzyme belongs to the serine/threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.

https://www.genecards.org/cgi-bin/carddisp.pl?gene=CAMK2A

https://www.genecards.org/cgi-bin/carddisp.pl?gene=CAMK2B

https://www.genecards.org/cgi-bin/carddisp.pl?gene=CAMK2G

https://www.genecards.org/cgi-bin/carddisp.pl?gene=CAMK2D

===Summary remarks===

===Structure===

===Action===

===Kinetics===

===References===

← Older revision		Revision as of 13:08, 16 April 2019
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		+	CaMKII undergoes multiple autoregulatory states that may have an impact on its function following Ca2+/CaM activation.
		+


	[[File: CaMKII,_Hudmon_2002,_CaMKII_undergoes_multiple_autoregulatory_states.png \| 600px \| CaMKII undergoes multiple autoregulatory states]]		[[File: CaMKII,_Hudmon_2002,_CaMKII_undergoes_multiple_autoregulatory_states.png \| 600px \| CaMKII undergoes multiple autoregulatory states]]

−	~~CaMKII undergoes multiple autoregulatory states that may have an impact on its function following Ca2+/CaM activation.~~
−

	The multimeric holoenzyme structure of CaMKII is depicted as a 6-mer for simplicity, with activated catalytic subunits illustrated in red. In addition to the Ca2+/CaM-dependent form of the enzyme phosphorylating physiological targets throughout the cell, autophosphorylation produces functional changes in CaMKII (autonomous activity, CaM trapping, CaM capping) that may alter further its activity, regulation, and function.		The multimeric holoenzyme structure of CaMKII is depicted as a 6-mer for simplicity, with activated catalytic subunits illustrated in red. In addition to the Ca2+/CaM-dependent form of the enzyme phosphorylating physiological targets throughout the cell, autophosphorylation produces functional changes in CaMKII (autonomous activity, CaM trapping, CaM capping) that may alter further its activity, regulation, and function.

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 Detection of multifunctional Ca2+–calmodulin-dependent kinase isoforms in human skeletal muscle. Rat brain (RB) and human skeletal muscle (HSkM) extract proteins were immunoblotted using isoform-specific CaM kinase antibodies. For skeletal muscle CaMKII the bands at 55–60 kDa probably correspond to γ/δ isoforms, whereas the 73 kDa band is likely to be the muscle-specific β isoform splice variant termed βM (Bayer et al. 1998; Damiani et al. 2000).
-The relative estimates of the amount of CaMKII isoforms in human skeletal muscle based on proteomics data from (Murgia 2017) <cite>2</cite> 28614723
+The relative estimates of the amount of CaMKII isoforms in human skeletal muscle based on proteomics data from (Murgia 2017) <cite>2</cite>
 {| class="wikitable"
 ! CaMKII subunit alpha