IndraLab

Statements


Catalytically active CALM1 activates CAMK4. 2 / 2
2 |

"OMIM summary: Human: Calmodulin is the archetype of the family of calcium-modulated proteins of which nearly 20 members have been found. They are identified by their occurrence in the cytosol or on membranes facing the cytosol and by a high affinity for calcium. Calmodulin contains 149 amino acids and has 4 calcium-binding domains. Its functions include roles in growth and the cell cycle as well as in signal transduction and the synthesis and release of neurotransmitters. Pubmed titles from omim summary: (summary is not available from this source) Entrez Gene GeneRifs summary: Human: Calmodulin is the archetype of the family of calcium-modulated proteins of which nearly 20 members have been found. They are identified by their occurrence in the cytosol or on membranes facing the cytosol and by a high affinity for calcium. Calmodulin contains 149 amino acids and has 4 calcium-binding domains. Its functions include roles in growth and the cell cycle as well as in signal transduction and the synthesis and release of neurotransmitters.[supplied by OMIM] Pubmed titles from gene summary: (summary is not available from this source) Jubilant PathArt summary: (summary is not available from this source) Ariadne Resnet summary: (summary is not available from this source) calcium/calmodulin activates calcium/calmodulin-dependent protein kinase I (CAMK1 Entrez gene list of calmodulin dependent proteins"

"Calcium is a well established regulator of transcription. Modulation of responses to this ubiquitous second messenger can occur by superposition of coincident Ca2+-independent signals, but there is also growing evidence that the strength, frequency, source, and location of the Ca2+ signal are determinants for specific transcriptional results. These complex variations must be translated into changes in protein function that preserve and process the information conveyed by the original signal. The Ca2+ receptor calmodulin (CaM)1 is involved in many of these changes through its effects on a variety of CaM-binding proteins (1). Among these, the multifunctional Ca2+/calmodulin-dependent protein kinases (CaMKs) are notable for their effects on components of transcription complexes, directly connecting Ca2+ with changes in gene expression. The highly homologous CaMKI and CaMKIV are distinct from the multimeric CaMKII, although all have broad and overlapping substrate preferences, because their activation is greatly enhanced following phosphorylation catalyzed by \"upstream\" kinases in a manner analogous to the mitogen-activated protein kinase cascade. Based on an evolving understanding of CaMKI/IV regulation and cloning of the CaMKI/IV kinases (CaMKKs), a Ca2+/CaM-dependent protein kinase I/IV cascade (CaMK cascade) has been proposed (2, 3). This review will discuss the biochemical and physiologic basis for the existence of this cascade and its potential for mediating Ca2+ regulation of transcription. Identification and Biochemical Characterization of a CaMK Cascade TOP INTRODUCTION Identification and Biochemical... Does the Cascade Function... Is the Cascade Physiologic? Other Transcriptional Targets... Evidence for a CaMK... REFERENCES CaMKI and CaMKIV are closely related protein kinases with many similarities in mode of activation and substrate preferences in vitro but with different tissue distributions. The kinases are regulated by Ca2+/CaM binding, which relieves intramolecular steric inhibition of the active site by a C-terminal autoinhibitory domain (Fig. 1)."