The phosphorylation state of threonine-220, a uniquely phosphatase-sensitive protein kinase a site in microtubule-associated protein MAP2c, regulates microtubule binding and stability

A. Alexa, G. Schmidt, P. Tompa, S. Ogueta, J. Vázquez, P. Kulcsár, J. Kovács, V. Dombrádi, P. Friedrich

Research output: Contribution to journalArticle

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Abstract

Phosphorylation of microtubule-associated protein 2 (MAP2) has a profound effect on microtubule stability and organization. In this work a consensus protein kinase A (PKA) phosphorylation site, T220, of juvenile MAP2c is characterized. As confirmed by mass spectrometry, this site can be phosphorylated by PKA but shows less than average reactivity among the 3.5 ± 0.5 phosphate residues incorporated into the protein. In contrast, T220 is uniquely sensitive to dephosphorylation: three major Ser/Thr protein phosphatases, in the order of efficiency PP2B > PP2Ac > PP1c, remove this phosphate group first. MAP2c specifically dephosphorylated at this site binds and stabilizes microtubules stronger than either fully phosphorylated or nonphosphorylated MAP2c. Phosphorylation of this site also affects proteolytic sensitivity of MAP2c, which might represent a further level of control in this system. Thus, the phosphorylation state of T220 may be a primary determinant of microtubule function.

Original languageEnglish
Pages (from-to)12427-12435
Number of pages9
JournalBiochemistry
Volume41
Issue number41
DOIs
Publication statusPublished - Oct 15 2002

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Phosphorylation
Microtubule-Associated Proteins
Threonine
Phosphoric Monoester Hydrolases
Microtubules
Protein Kinases
Cyclic AMP-Dependent Protein Kinases
Phosphates
Phosphoprotein Phosphatases
Mass spectrometry
Mass Spectrometry
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

The phosphorylation state of threonine-220, a uniquely phosphatase-sensitive protein kinase a site in microtubule-associated protein MAP2c, regulates microtubule binding and stability. / Alexa, A.; Schmidt, G.; Tompa, P.; Ogueta, S.; Vázquez, J.; Kulcsár, P.; Kovács, J.; Dombrádi, V.; Friedrich, P.

In: Biochemistry, Vol. 41, No. 41, 15.10.2002, p. 12427-12435.

Research output: Contribution to journalArticle

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abstract = "Phosphorylation of microtubule-associated protein 2 (MAP2) has a profound effect on microtubule stability and organization. In this work a consensus protein kinase A (PKA) phosphorylation site, T220, of juvenile MAP2c is characterized. As confirmed by mass spectrometry, this site can be phosphorylated by PKA but shows less than average reactivity among the 3.5 ± 0.5 phosphate residues incorporated into the protein. In contrast, T220 is uniquely sensitive to dephosphorylation: three major Ser/Thr protein phosphatases, in the order of efficiency PP2B > PP2Ac > PP1c, remove this phosphate group first. MAP2c specifically dephosphorylated at this site binds and stabilizes microtubules stronger than either fully phosphorylated or nonphosphorylated MAP2c. Phosphorylation of this site also affects proteolytic sensitivity of MAP2c, which might represent a further level of control in this system. Thus, the phosphorylation state of T220 may be a primary determinant of microtubule function.",
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T1 - The phosphorylation state of threonine-220, a uniquely phosphatase-sensitive protein kinase a site in microtubule-associated protein MAP2c, regulates microtubule binding and stability

AU - Alexa, A.

AU - Schmidt, G.

AU - Tompa, P.

AU - Ogueta, S.

AU - Vázquez, J.

AU - Kulcsár, P.

AU - Kovács, J.

AU - Dombrádi, V.

AU - Friedrich, P.

PY - 2002/10/15

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N2 - Phosphorylation of microtubule-associated protein 2 (MAP2) has a profound effect on microtubule stability and organization. In this work a consensus protein kinase A (PKA) phosphorylation site, T220, of juvenile MAP2c is characterized. As confirmed by mass spectrometry, this site can be phosphorylated by PKA but shows less than average reactivity among the 3.5 ± 0.5 phosphate residues incorporated into the protein. In contrast, T220 is uniquely sensitive to dephosphorylation: three major Ser/Thr protein phosphatases, in the order of efficiency PP2B > PP2Ac > PP1c, remove this phosphate group first. MAP2c specifically dephosphorylated at this site binds and stabilizes microtubules stronger than either fully phosphorylated or nonphosphorylated MAP2c. Phosphorylation of this site also affects proteolytic sensitivity of MAP2c, which might represent a further level of control in this system. Thus, the phosphorylation state of T220 may be a primary determinant of microtubule function.

AB - Phosphorylation of microtubule-associated protein 2 (MAP2) has a profound effect on microtubule stability and organization. In this work a consensus protein kinase A (PKA) phosphorylation site, T220, of juvenile MAP2c is characterized. As confirmed by mass spectrometry, this site can be phosphorylated by PKA but shows less than average reactivity among the 3.5 ± 0.5 phosphate residues incorporated into the protein. In contrast, T220 is uniquely sensitive to dephosphorylation: three major Ser/Thr protein phosphatases, in the order of efficiency PP2B > PP2Ac > PP1c, remove this phosphate group first. MAP2c specifically dephosphorylated at this site binds and stabilizes microtubules stronger than either fully phosphorylated or nonphosphorylated MAP2c. Phosphorylation of this site also affects proteolytic sensitivity of MAP2c, which might represent a further level of control in this system. Thus, the phosphorylation state of T220 may be a primary determinant of microtubule function.

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