Phosphorylation of Microtubule-Associated Proteins (MAPs) and pH of the Medium Control Interaction between MAPs and Actin Filaments

Interaction of microtubule-associated proteins (MAPs) with actin filaments at neutral pH is inhibited by phosphorylation of MAPs. Phosphorylated MAPs are less potent than unphosphorylated ones in increasing the low-shear viscosity of actin filaments in the neutral pH range. The ability of unphosphor...

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Published inJournal of biochemistry (Tokyo) Vol. 90; no. 2; pp. 575 - 578
Main Authors NISHIDA, Eisuke, KUWAKI, Tomoyuki, SAKAI, Hikoichi
Format Journal Article
LanguageEnglish
Published England Oxford University Press 01.01.1981
Subjects
actin
Actins - metabolism
Animals
Hydrogen-Ion Concentration
Microtubule-Associated Proteins
microtubules
Microtubules - metabolism
pH effects
Phosphorylation
proteins
Proteins - metabolism
Rabbits
Swine
Tubulin - metabolism
Viscosity
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Summary:Interaction of microtubule-associated proteins (MAPs) with actin filaments at neutral pH is inhibited by phosphorylation of MAPs. Phosphorylated MAPs are less potent than unphosphorylated ones in increasing the low-shear viscosity of actin filaments in the neutral pH range. The ability of unphosphorylated MAPs to crosslink actin filaments falls off sharply above pH 7.5. Upon phosphorylation, the crosslinking ability of the MAPs peaks sharply between pH 6.2 and 6.3. Thus, the MAPs-actin interaction can be regulated by phosphorylation of MAPs and small changes in the physiological range of pH.
Bibliography:1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan (No. 444074).
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ArticleID:90.2.575
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content type line 23
ISSN:0021-924X
DOI:10.1093/oxfordjournals.jbchem.a133510