Biomaterial Database

Activation of Ca(2+)-calmodulin-dependent protein kinase Ia is due to direct phosphorylation by its activator. 1995

J C Lee, and A M Edelman

Department of Pharmacology and Toxicology, State University of New York at Buffalo, New York 14214, USA.

Ca(2+)-Calmodulin-dependent protein kinase Ia (CaM kinase Ia) is phosphorylated, and its activity enhanced up to 50-fold, in the presence of a protein purified from pig brain termed CaM kinase Ia activator [Lee, J.C. and Edelman, A.M. (1994) J. Biol. Chem. 269, 2158-2164]. We report here that phosphorylation of CaM kinase Ia in the presence of the activator occurs primarily on threonine (87%) and slightly on serine (13%) residues. Treatment of CaM kinase Ia with the irreversible ATP affinity analogue, 5'-p-fluorosulfonylbenzoyl adenosine (FSBA), reduces its activity by 86% but has no effect on its ability to be phosphorylated, whereas FSBA-treatment of the activator reduces its ability to activate and phosphorylate CaM kinase Ia by 92 and 93%, respectively. Thus, CaM kinase Ia activator is a protein Thr/Ser kinase which activates by phosphorylating CaM kinase Ia rather than by enhancing the latter's autophosphorylation.

UI	MeSH Term	Description	Entries
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010766	Phosphorylation	The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.	Phosphorylations
D011494	Protein Kinases	A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.	Protein Kinase,Kinase, Protein,Kinases, Protein
D004789	Enzyme Activation	Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.	Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D000241	Adenosine	A nucleoside that is composed of ADENINE and D-RIBOSE. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. Adenosine itself is a neurotransmitter.	Adenocard,Adenoscan
D000345	Affinity Labels	Analogs of those substrates or compounds which bind naturally at the active sites of proteins, enzymes, antibodies, steroids, or physiological receptors. These analogs form a stable covalent bond at the binding site, thereby acting as inhibitors of the proteins or steroids.	Affinity Labeling Reagents,Labeling Reagents, Affinity,Labels, Affinity,Reagents, Affinity Labeling
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013552	Swine	Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).	Phacochoerus,Pigs,Suidae,Warthogs,Wart Hogs,Hog, Wart,Hogs, Wart,Wart Hog
D017871	Calcium-Calmodulin-Dependent Protein Kinases	A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)	Ca(2+)-Calmodulin-Dependent Protein Kinase,Calcium-Calmodulin-Dependent Protein Kinase,Calmodulin-Dependent Protein Kinase,Calmodulin-Dependent Protein Kinases,Multifunctional Calcium-Calmodulin-Dependent Protein Kinase,Restricted Calcium-Calmodulin-Dependent Protein Kinase,Calcium-Calmodulin-Dependent Protein Kinases, Multifunctional,Calcium-Calmodulin-Dependent Protein Kinases, Restricted,Calmodulin-Dependent Multiprotein Kinase,Calmodulin-Kinase,Cam-MPK,Multifunctional Calcium-Calmodulin-Dependent Protein Kinases,Restricted Calcium-Calmodulin-Dependent Protein Kinases,Calcium Calmodulin Dependent Protein Kinase,Calcium Calmodulin Dependent Protein Kinases, Multifunctional,Calcium Calmodulin Dependent Protein Kinases, Restricted,Calmodulin Dependent Multiprotein Kinase,Calmodulin Dependent Protein Kinase,Calmodulin Dependent Protein Kinases,Calmodulin Kinase,Cam MPK,Kinase, Calcium-Calmodulin-Dependent Protein,Kinase, Calmodulin-Dependent Protein,Multifunctional Calcium Calmodulin Dependent Protein Kinase,Multifunctional Calcium Calmodulin Dependent Protein Kinases,Multiprotein Kinase, Calmodulin-Dependent,Protein Kinase, Calcium-Calmodulin-Dependent,Protein Kinase, Calmodulin-Dependent,Protein Kinases, Calcium-Calmodulin-Dependent,Protein Kinases, Calmodulin-Dependent,Restricted Calcium Calmodulin Dependent Protein Kinase,Restricted Calcium Calmodulin Dependent Protein Kinases