Identification of the multifunctional calmodulin-dependent protein kinase in the cytosol, sarcoplasmic reticulum, and sarcolemma of rabbit skeletal muscle

Hiroshi Sato; Kohji Fukunaga; Shukuro Araki; Iwao Ohtsuki; Eishichi Miyamoto

doi:10.1016/0003-9861(88)90468-7

Identification of the multifunctional calmodulin-dependent protein kinase in the cytosol, sarcoplasmic reticulum, and sarcolemma of rabbit skeletal muscle

Hiroshi Sato, Kohji Fukunaga, Shukuro Araki, Iwao Ohtsuki, Eishichi Miyamoto

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

Abstract

A multifunctional calmodulin-dependent protein kinase (calmodulin kinase) was purified from the cytosol of rabbit skeletal muscle as a subunit of 58 kDa. A 58-kDa protein in sarcoplasmic reticulum (SR) and sarcolemma (SL) of rabbit skeletal muscle was endogenously phosphorylated in a calmodulin-dependent manner. The 58-kDa protein in SR and SL was considered to be identical to the subunit of cytosol calmodulin kinase on the basis of immunoreactivity, calmodulin binding, and autophosphorylation studies and on the patterns of protease-treated phosphopeptides. Calmodulin kinase showed broad substrate specificity and phosphorylated troponins I and T.

Original language	English
Pages (from-to)	443-451
Number of pages	9
Journal	Archives of Biochemistry and Biophysics
Volume	260
Issue number	1
DOIs	https://doi.org/10.1016/0003-9861(88)90468-7
Publication status	Published - 1988 Jan
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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10.1016/0003-9861(88)90468-7

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title = "Identification of the multifunctional calmodulin-dependent protein kinase in the cytosol, sarcoplasmic reticulum, and sarcolemma of rabbit skeletal muscle",

abstract = "A multifunctional calmodulin-dependent protein kinase (calmodulin kinase) was purified from the cytosol of rabbit skeletal muscle as a subunit of 58 kDa. A 58-kDa protein in sarcoplasmic reticulum (SR) and sarcolemma (SL) of rabbit skeletal muscle was endogenously phosphorylated in a calmodulin-dependent manner. The 58-kDa protein in SR and SL was considered to be identical to the subunit of cytosol calmodulin kinase on the basis of immunoreactivity, calmodulin binding, and autophosphorylation studies and on the patterns of protease-treated phosphopeptides. Calmodulin kinase showed broad substrate specificity and phosphorylated troponins I and T.",

author = "Hiroshi Sato and Kohji Fukunaga and Shukuro Araki and Iwao Ohtsuki and Eishichi Miyamoto",

note = "Funding Information: {\textquoteright} This research was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan (61115002) and a Grant (86-03-40) from the National Center of Neurology and Psychiatry (NCNP) from the Ministry of Health and Welfare of Japan. {\textquoteright} To whom correspondence should be addressed.",

year = "1988",

month = jan,

doi = "10.1016/0003-9861(88)90468-7",

language = "English",

volume = "260",

pages = "443--451",

journal = "Archives of Biochemistry and Biophysics",

issn = "0003-9861",

publisher = "Academic Press Inc.",

number = "1",

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TY - JOUR

T1 - Identification of the multifunctional calmodulin-dependent protein kinase in the cytosol, sarcoplasmic reticulum, and sarcolemma of rabbit skeletal muscle

AU - Sato, Hiroshi

AU - Fukunaga, Kohji

AU - Araki, Shukuro

AU - Ohtsuki, Iwao

AU - Miyamoto, Eishichi

N1 - Funding Information: ’ This research was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan (61115002) and a Grant (86-03-40) from the National Center of Neurology and Psychiatry (NCNP) from the Ministry of Health and Welfare of Japan. ’ To whom correspondence should be addressed.

PY - 1988/1

Y1 - 1988/1

N2 - A multifunctional calmodulin-dependent protein kinase (calmodulin kinase) was purified from the cytosol of rabbit skeletal muscle as a subunit of 58 kDa. A 58-kDa protein in sarcoplasmic reticulum (SR) and sarcolemma (SL) of rabbit skeletal muscle was endogenously phosphorylated in a calmodulin-dependent manner. The 58-kDa protein in SR and SL was considered to be identical to the subunit of cytosol calmodulin kinase on the basis of immunoreactivity, calmodulin binding, and autophosphorylation studies and on the patterns of protease-treated phosphopeptides. Calmodulin kinase showed broad substrate specificity and phosphorylated troponins I and T.

AB - A multifunctional calmodulin-dependent protein kinase (calmodulin kinase) was purified from the cytosol of rabbit skeletal muscle as a subunit of 58 kDa. A 58-kDa protein in sarcoplasmic reticulum (SR) and sarcolemma (SL) of rabbit skeletal muscle was endogenously phosphorylated in a calmodulin-dependent manner. The 58-kDa protein in SR and SL was considered to be identical to the subunit of cytosol calmodulin kinase on the basis of immunoreactivity, calmodulin binding, and autophosphorylation studies and on the patterns of protease-treated phosphopeptides. Calmodulin kinase showed broad substrate specificity and phosphorylated troponins I and T.

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DO - 10.1016/0003-9861(88)90468-7

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VL - 260

SP - 443

EP - 451

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 1

ER -

Identification of the multifunctional calmodulin-dependent protein kinase in the cytosol, sarcoplasmic reticulum, and sarcolemma of rabbit skeletal muscle

Abstract

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