Warning: Undefined variable $zfal in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Deprecated: str_replace(): Passing null to parameter #3 ($subject) of type array|string is deprecated in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 530
free
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 531
free free
English Wikipedia
Nephropedia Template TP (
Twit Text
DeepDyve Pubget Overpricing |
lüll The ss subunit of voltage-gated Ca2+ channels Buraei Z; Yang JPhysiol Rev 2010[Oct]; 90 (4): 1461-506Calcium regulates a wide spectrum of physiological processes such as heartbeat, muscle contraction, neuronal communication, hormone release, cell division, and gene transcription. Major entryways for Ca(2+) in excitable cells are high-voltage activated (HVA) Ca(2+) channels. These are plasma membrane proteins composed of several subunits, including alpha(1), alpha(2)delta, beta, and gamma. Although the principal alpha(1) subunit (Ca(v)alpha(1)) contains the channel pore, gating machinery and most drug binding sites, the cytosolic auxiliary beta subunit (Ca(v)beta) plays an essential role in regulating the surface expression and gating properties of HVA Ca(2+) channels. Ca(v)beta is also crucial for the modulation of HVA Ca(2+) channels by G proteins, kinases, and the Ras-related RGK GTPases. New proteins have emerged in recent years that modulate HVA Ca(2+) channels by binding to Ca(v)beta. There are also indications that Ca(v)beta may carry out Ca(2+) channel-independent functions, including directly regulating gene transcription. All four subtypes of Ca(v)beta, encoded by different genes, have a modular organization, consisting of three variable regions, a conserved guanylate kinase (GK) domain, and a conserved Src-homology 3 (SH3) domain, placing them into the membrane-associated guanylate kinase (MAGUK) protein family. Crystal structures of Ca(v)betas reveal how they interact with Ca(v)alpha(1), open new research avenues, and prompt new inquiries. In this article, we review the structure and various biological functions of Ca(v)beta, with both a historical perspective as well as an emphasis on recent advances.|Amino Acid Sequence[MESH]|Animals[MESH]|Calcium Channels/chemistry/genetics/*metabolism[MESH]|Humans[MESH]|Ion Channel Gating/*physiology[MESH]|Protein Conformation[MESH]|Protein Subunits[MESH] |