Literature DB >> 2549640

Primary structure of the beta subunit of the DHP-sensitive calcium channel from skeletal muscle.

P Ruth1, A Röhrkasten, M Biel, E Bosse, S Regulla, H E Meyer, V Flockerzi, F Hofmann.   

Abstract

Complementary DNAs for the beta subunit of the dihydropyridine-sensitive calcium channel of rabbit skeletal muscle were isolated on the basis of peptide sequences derived from the purified protein. The deduced primary structure is without homology to other known protein sequences and is consistent with the beta subunit being a peripheral membrane protein associated with the cytoplasmic aspect of the sarcolemma. The protein contains sites that might be expected to be preferentially phosphorylated by protein kinase C and guanosine 3',5'-monophosphate-dependent protein kinase. A messenger RNA for this protein appears to be expressed in brain.

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Year:  1989        PMID: 2549640     DOI: 10.1126/science.2549640

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  81 in total

1.  Involvement of the carboxy-terminus region of the dihydropyridine receptor beta1a subunit in excitation-contraction coupling of skeletal muscle.

Authors:  M Beurg; C A Ahern; P Vallejo; M W Conklin; P A Powers; R G Gregg; R Coronado
Journal:  Biophys J       Date:  1999-12       Impact factor: 4.033

2.  Differential regulation of skeletal muscle L-type Ca2+ current and excitation-contraction coupling by the dihydropyridine receptor beta subunit.

Authors:  M Beurg; M Sukhareva; C A Ahern; M W Conklin; E Perez-Reyes; P A Powers; R G Gregg; R Coronado
Journal:  Biophys J       Date:  1999-04       Impact factor: 4.033

3.  Novel functional properties of Ca(2+) channel beta subunits revealed by their expression in adult rat heart cells.

Authors:  Henry M Colecraft; Badr Alseikhan; Shoji X Takahashi; Dipayan Chaudhuri; Scott Mittman; Vasan Yegnasubramanian; Rebecca S Alvania; David C Johns; Eduardo Marbán; David T Yue
Journal:  J Physiol       Date:  2002-06-01       Impact factor: 5.182

4.  Current modulation and membrane targeting of the calcium channel alpha1C subunit are independent functions of the beta subunit.

Authors:  U Gerster; B Neuhuber; K Groschner; J Striessnig; B E Flucher
Journal:  J Physiol       Date:  1999-06-01       Impact factor: 5.182

5.  Rab3-interacting molecule gamma isoforms lacking the Rab3-binding domain induce long lasting currents but block neurotransmitter vesicle anchoring in voltage-dependent P/Q-type Ca2+ channels.

Authors:  Yoshitsugu Uriu; Shigeki Kiyonaka; Takafumi Miki; Masakuni Yagi; Satoshi Akiyama; Emiko Mori; Akito Nakao; Aaron M Beedle; Kevin P Campbell; Minoru Wakamori; Yasuo Mori
Journal:  J Biol Chem       Date:  2010-05-07       Impact factor: 5.157

6.  Differential modulation of cardiac Ca2+ channel gating by beta-subunits.

Authors:  Igor Dzhura; Alan Neely
Journal:  Biophys J       Date:  2003-07       Impact factor: 4.033

7.  Structures of the murine genes for the beta1- and beta4-subunits of the voltage-dependent calcium channel.

Authors:  Manabu Murakami; Ichiro Miyoshi; Takashi Suzuki; Hironobu Sasano; Toshihiko Iijima
Journal:  J Mol Neurosci       Date:  2003       Impact factor: 3.444

8.  The synaptic vesicle protein synaptotagmin associates with calcium channels and is a putative Lambert-Eaton myasthenic syndrome antigen.

Authors:  C Leveque; T Hoshino; P David; Y Shoji-Kasai; K Leys; A Omori; B Lang; O el Far; K Sato; N Martin-Moutot
Journal:  Proc Natl Acad Sci U S A       Date:  1992-04-15       Impact factor: 11.205

9.  Subunits of purified calcium channels: a 212-kDa form of alpha 1 and partial amino acid sequence of a phosphorylation site of an independent beta subunit.

Authors:  K S De Jongh; D K Merrick; W A Catterall
Journal:  Proc Natl Acad Sci U S A       Date:  1989-11       Impact factor: 11.205

10.  Regulation of the calcium slow channel by cyclic GMP dependent protein kinase in chick heart cells.

Authors:  G E Haddad; N Sperelakis; G Bkaily
Journal:  Mol Cell Biochem       Date:  1995-07-05       Impact factor: 3.396

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