Phosphorylation and actin activation of brain myosin.

B. Barylko; A. Sobieszek

doi:10.1002/j.1460-2075.1983.tb01432.x

Phosphorylation and actin activation of brain myosin.

B. Barylko, A. Sobieszek

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

19 Scopus citations

Abstract

A method is described for obtaining brain myosin that shows significant actin activation, after phosphorylation with chicken gizzard myosin light chain kinase. Myosin with this activity could be obtained only via the initial purification of brain actomyosin. The latter complex, isolated by a method similar to that used for smooth muscle, contained actin, myosin, tropomyosin of the non-muscle type and another actin-binding protein of approximately 100,000 daltons. From the presence of a specific myosin light chain kinase and phosphatase in brain tissue it is suggested that the regulation of actin-myosin interaction operates via phosphorylation and dephosphorylation of myosin.

Original language	English (US)
Pages (from-to)	369-374
Number of pages	6
Journal	The EMBO journal
Volume	2
Issue number	3
DOIs	https://doi.org/10.1002/j.1460-2075.1983.tb01432.x
State	Published - 1983

ASJC Scopus subject areas

General Neuroscience
Molecular Biology
General Biochemistry, Genetics and Molecular Biology
General Immunology and Microbiology

Access to Document

10.1002/j.1460-2075.1983.tb01432.x

Cite this

@article{144619cebddd413f876d40512d20e41f,

title = "Phosphorylation and actin activation of brain myosin.",

abstract = "A method is described for obtaining brain myosin that shows significant actin activation, after phosphorylation with chicken gizzard myosin light chain kinase. Myosin with this activity could be obtained only via the initial purification of brain actomyosin. The latter complex, isolated by a method similar to that used for smooth muscle, contained actin, myosin, tropomyosin of the non-muscle type and another actin-binding protein of approximately 100,000 daltons. From the presence of a specific myosin light chain kinase and phosphatase in brain tissue it is suggested that the regulation of actin-myosin interaction operates via phosphorylation and dephosphorylation of myosin.",

author = "B. Barylko and A. Sobieszek",

note = "Copyright: This record is sourced from MEDLINE/PubMed, a database of the U.S. National Library of Medicine",

year = "1983",

doi = "10.1002/j.1460-2075.1983.tb01432.x",

language = "English (US)",

volume = "2",

pages = "369--374",

journal = "The EMBO journal",

issn = "0261-4189",

publisher = "Nature Publishing Group",

number = "3",

}

TY - JOUR

T1 - Phosphorylation and actin activation of brain myosin.

AU - Barylko, B.

AU - Sobieszek, A.

N1 - Copyright: This record is sourced from MEDLINE/PubMed, a database of the U.S. National Library of Medicine

PY - 1983

Y1 - 1983

N2 - A method is described for obtaining brain myosin that shows significant actin activation, after phosphorylation with chicken gizzard myosin light chain kinase. Myosin with this activity could be obtained only via the initial purification of brain actomyosin. The latter complex, isolated by a method similar to that used for smooth muscle, contained actin, myosin, tropomyosin of the non-muscle type and another actin-binding protein of approximately 100,000 daltons. From the presence of a specific myosin light chain kinase and phosphatase in brain tissue it is suggested that the regulation of actin-myosin interaction operates via phosphorylation and dephosphorylation of myosin.

AB - A method is described for obtaining brain myosin that shows significant actin activation, after phosphorylation with chicken gizzard myosin light chain kinase. Myosin with this activity could be obtained only via the initial purification of brain actomyosin. The latter complex, isolated by a method similar to that used for smooth muscle, contained actin, myosin, tropomyosin of the non-muscle type and another actin-binding protein of approximately 100,000 daltons. From the presence of a specific myosin light chain kinase and phosphatase in brain tissue it is suggested that the regulation of actin-myosin interaction operates via phosphorylation and dephosphorylation of myosin.

UR - http://www.scopus.com/inward/record.url?scp=0021092954&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021092954&partnerID=8YFLogxK

U2 - 10.1002/j.1460-2075.1983.tb01432.x

DO - 10.1002/j.1460-2075.1983.tb01432.x

M3 - Article

C2 - 11894951

AN - SCOPUS:0021092954

SN - 0261-4189

VL - 2

SP - 369

EP - 374

JO - The EMBO journal

JF - The EMBO journal

IS - 3

ER -

Phosphorylation and actin activation of brain myosin.

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this