Dephosphorylation of distinct sites on microtubule-associated protein MAP1B by protein phosphatases 1, 2A and 2B

Luis Ulloa; Viktor Dombrádi; Javier Díaz-Nido; Kornélia Szücs; Pál Gergely; Peter Friedrich; Jesus Avila

doi:10.1016/0014-5793(93)80925-K

Dephosphorylation of distinct sites on microtubule-associated protein MAP1B by protein phosphatases 1, 2A and 2B

Luis Ulloa, Viktor Dombrádi, Javier Díaz-Nido, Kornélia Szücs, Pál Gergely, Peter Friedrich, Jesus Avila

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

48 Scopus citations

Abstract

Rat brain microtubule-associated protein MAP1 B has been tested as a substrate for Ser/Thr protein phosphatases (PP). The dephosphorylation reactions were followed by specific antibodies recognizing phosphorylated and phosphorylatable epitopes. One set of phosphorylation sites on MAPI B are referred to as mode I sites, and their phosphorylation is presumably catalyzed by proline-directed protein kinases. These mode I sites are efficiently dephosphorylated by PP2B and 2A but not by PP1. Another set of phosphorylation sites on MAP1B are named mode II sites, and their phosphorylation is possibly due to casein kinase II. These mode II sites are dephosphorylated by PP2A and PP1, the PP2B being ineffective. The selectivity of phosphatases for different sites within the same protein indicates the complexity of the dephosphorylation reactions regulating the functionality of MAP1B in neurons.

Original language	English (US)
Pages (from-to)	85-89
Number of pages	5
Journal	FEBS Letters
Volume	330
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(93)80925-K
State	Published - Sep 6 1993
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Keywords

CaScin kinase II (CKII)
Calcineurin
Microtubule-associated protein
Phosphorylation/dephosphorylation
Proline direct protein kinase (PDPK)
Protein phosphatase 1 and 2A

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10.1016/0014-5793(93)80925-K

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title = "Dephosphorylation of distinct sites on microtubule-associated protein MAP1B by protein phosphatases 1, 2A and 2B",

abstract = "Rat brain microtubule-associated protein MAP1 B has been tested as a substrate for Ser/Thr protein phosphatases (PP). The dephosphorylation reactions were followed by specific antibodies recognizing phosphorylated and phosphorylatable epitopes. One set of phosphorylation sites on MAPI B are referred to as mode I sites, and their phosphorylation is presumably catalyzed by proline-directed protein kinases. These mode I sites are efficiently dephosphorylated by PP2B and 2A but not by PP1. Another set of phosphorylation sites on MAP1B are named mode II sites, and their phosphorylation is possibly due to casein kinase II. These mode II sites are dephosphorylated by PP2A and PP1, the PP2B being ineffective. The selectivity of phosphatases for different sites within the same protein indicates the complexity of the dephosphorylation reactions regulating the functionality of MAP1B in neurons.",

keywords = "CaScin kinase II (CKII), Calcineurin, Microtubule-associated protein, Phosphorylation/dephosphorylation, Proline direct protein kinase (PDPK), Protein phosphatase 1 and 2A",

author = "Luis Ulloa and Viktor Dombr{\'a}di and Javier D{\'i}az-Nido and Korn{\'e}lia Sz{\"u}cs and P{\'a}l Gergely and Peter Friedrich and Jesus Avila",

note = "Funding Information: Ackno~vlr~~en7ents:T his work has been supported by grants OTKA 1501 and ETT-T-IO/T-460 to PC and by OTKA 1364 grant to P.F., from the Hungarran Academy of Scrence and from the Hungarian Mmrstry of Health, as well as by a Spamsh CICYT grant to J.A.",

year = "1993",

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doi = "10.1016/0014-5793(93)80925-K",

language = "English (US)",

volume = "330",

pages = "85--89",

journal = "FEBS Letters",

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T1 - Dephosphorylation of distinct sites on microtubule-associated protein MAP1B by protein phosphatases 1, 2A and 2B

AU - Ulloa, Luis

AU - Dombrádi, Viktor

AU - Díaz-Nido, Javier

AU - Szücs, Kornélia

AU - Gergely, Pál

AU - Friedrich, Peter

AU - Avila, Jesus

N1 - Funding Information: Ackno~vlr~~en7ents:T his work has been supported by grants OTKA 1501 and ETT-T-IO/T-460 to PC and by OTKA 1364 grant to P.F., from the Hungarran Academy of Scrence and from the Hungarian Mmrstry of Health, as well as by a Spamsh CICYT grant to J.A.

PY - 1993/9/6

Y1 - 1993/9/6

N2 - Rat brain microtubule-associated protein MAP1 B has been tested as a substrate for Ser/Thr protein phosphatases (PP). The dephosphorylation reactions were followed by specific antibodies recognizing phosphorylated and phosphorylatable epitopes. One set of phosphorylation sites on MAPI B are referred to as mode I sites, and their phosphorylation is presumably catalyzed by proline-directed protein kinases. These mode I sites are efficiently dephosphorylated by PP2B and 2A but not by PP1. Another set of phosphorylation sites on MAP1B are named mode II sites, and their phosphorylation is possibly due to casein kinase II. These mode II sites are dephosphorylated by PP2A and PP1, the PP2B being ineffective. The selectivity of phosphatases for different sites within the same protein indicates the complexity of the dephosphorylation reactions regulating the functionality of MAP1B in neurons.

AB - Rat brain microtubule-associated protein MAP1 B has been tested as a substrate for Ser/Thr protein phosphatases (PP). The dephosphorylation reactions were followed by specific antibodies recognizing phosphorylated and phosphorylatable epitopes. One set of phosphorylation sites on MAPI B are referred to as mode I sites, and their phosphorylation is presumably catalyzed by proline-directed protein kinases. These mode I sites are efficiently dephosphorylated by PP2B and 2A but not by PP1. Another set of phosphorylation sites on MAP1B are named mode II sites, and their phosphorylation is possibly due to casein kinase II. These mode II sites are dephosphorylated by PP2A and PP1, the PP2B being ineffective. The selectivity of phosphatases for different sites within the same protein indicates the complexity of the dephosphorylation reactions regulating the functionality of MAP1B in neurons.

KW - CaScin kinase II (CKII)

KW - Calcineurin

KW - Microtubule-associated protein

KW - Phosphorylation/dephosphorylation

KW - Proline direct protein kinase (PDPK)

KW - Protein phosphatase 1 and 2A

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Dephosphorylation of distinct sites on microtubule-associated protein MAP1B by protein phosphatases 1, 2A and 2B

Abstract

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