Structural basis of binding the unique N-terminal domain of
microtubule-associated protein 2c to proteins regulating
kinases of signaling pathways

J 2024

Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways

BARTOŠÍK, Viktor; Jitka PLUCAROVÁ; Alice LANÍKOVÁ; Zuzana JANÁČKOVÁ; Petr PADRTA et. al.

Basic information

Original name

Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways

Authors

BARTOŠÍK, Viktor (203 Czech Republic, belonging to the institution); Jitka PLUCAROVÁ (203 Czech Republic, belonging to the institution); Alice LANÍKOVÁ (203 Czech Republic, belonging to the institution); Zuzana JANÁČKOVÁ (203 Czech Republic, belonging to the institution); Petr PADRTA (203 Czech Republic, belonging to the institution); Séverine JANSEN (250 France, belonging to the institution); Tobias GRUBER; Vojtěch VAŘEČKA (203 Czech Republic, belonging to the institution); Stephan M FELLER and Lukáš ŽÍDEK (203 Czech Republic, belonging to the institution)

Edition

International Journal of Biological Chemistry, AMSTERDAM, ANSInet, 2024, 0021-9258

Other information

Language

English

Type of outcome

Article in a journal

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Netherlands

Confidentiality degree

is not subject to a state or trade secret

References:

URL

Impact factor

Impact factor: 4.000 in 2023

RIV identification code

RIV/00216224:14740/24:00138072

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1016/j.jbc.2024.107551

UT WoS

001365739800001

EID Scopus

2-s2.0-85200983503

Keywords in English

GENERAL FORCE-FIELD; A ANCHORING PROTEIN; TYROSINE PHOSPHORYLATION; SECONDARY STRUCTURE; DIPOLAR COUPLINGS; HETERONUCLEAR NMR; AKAP SPECIFICITY; MAP2 EXPRESSION; LARGER PROTEINS; SH2 DOMAIN

Abstract

V originále

Isoforms of microtubule-associated protein 2 (MAP2) differ from their homolog Tau in the sequence and interactions of the N-terminal region. Binding of the N-terminal region of MAP2c (N-MAP2c) to the dimerization/docking domains of the regulatory subunit RIIa of cAMP-dependent protein kinase (RIIDD2) and to the Src-homology domain 2 (SH2) of growth factor receptor-bound protein 2 (Grb2) have been described long time ago. However, the structural features of the complexes remained unknown due to the disordered nature of MAP2. Here, we provide structural description of the complexes. We have solved solution structure of N-MAP2c in complex with RIIDD2, confirming formation of an amphiphilic a-helix of MAP2c upon binding, defining orientation of the ahelix in the complex and showing that its binding register differs from previous predictions. Using chemical shift mapping, we characterized the binding interface of SH2-Grb2 and rat MAP2c phosphorylated by the tyrosine kinase Fyn in their complex and proposed a model explaining differences between SH2-Grb2 complexes with rat MAP2c and phosphopeptides with a Grb2-specific sequence. The results provide the structural basis of a potential role of MAP2 in regulating cAMPdependent phosphorylation cascade via interactions with RIIDD2 and Ras signaling pathway via interactions with SH2

Links

EF18_046/0015974, research and development project

Name: Modernizace České infrastruktury pro integrativní strukturní biologii

GA20-12669S, research and development project

Name: Interakce určující fyziologické funkce proteinu Microtubule Associated Protein 2c s atomovým rozlišením

Investor: Czech Science Foundation

MUNI/A/1641/2023, interní kód MU

Name: Struktura a dynamika biopolymerů

Investor: Masaryk University

90242, large research infrastructures

Name: CIISB III

Cite

BARTOŠÍK, Viktor; Jitka PLUCAROVÁ; Alice LANÍKOVÁ; Zuzana JANÁČKOVÁ; Petr PADRTA; Séverine JANSEN; Tobias GRUBER; Vojtěch VAŘEČKA; Stephan M FELLER and Lukáš ŽÍDEK. Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways. International Journal of Biological Chemistry. AMSTERDAM: ANSInet, 2024, vol. 300, No 8, p. 1-22. ISSN 0021-9258. Available from: https://dx.doi.org/10.1016/j.jbc.2024.107551.

@article{2461539,
   author = {Bartošík, Viktor and Plucarová, Jitka and Laníková, Alice and Janáčková, Zuzana and Padrta, Petr and Jansen, Séverine and Gruber, Tobias and Vařečka, Vojtěch and Feller, Stephan M and Žídek, Lukáš},
   article_location = {AMSTERDAM},
   article_number = {8},
   doi = {http://dx.doi.org/10.1016/j.jbc.2024.107551},
   keywords = {GENERAL FORCE-FIELD; A ANCHORING PROTEIN; TYROSINE PHOSPHORYLATION; SECONDARY STRUCTURE; DIPOLAR COUPLINGS; HETERONUCLEAR NMR; AKAP SPECIFICITY; MAP2 EXPRESSION; LARGER PROTEINS; SH2 DOMAIN},
   language = {eng},
   issn = {0021-9258},
   journal = {International Journal of Biological Chemistry},
   title = {Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways},
   url = {https://www.jbc.org/article/S0021-9258(24)02052-0/fulltext},
   volume = {300},
   year = {2024}
}

TY  - JOUR
ID  - 2461539
AU  - Bartošík, Viktor - Plucarová, Jitka - Laníková, Alice - Janáčková, Zuzana - Padrta, Petr - Jansen, Séverine - Gruber, Tobias - Vařečka, Vojtěch - Feller, Stephan M - Žídek, Lukáš
PY  - 2024
TI  - Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways
JF  - International Journal of Biological Chemistry
VL  - 300
IS  - 8
SP  - 1-22
EP  - 1-22
PB  - ANSInet
SN  - 00219258
KW  - GENERAL FORCE-FIELD
KW  - A ANCHORING PROTEIN
KW  - TYROSINE PHOSPHORYLATION
KW  - SECONDARY STRUCTURE
KW  - DIPOLAR COUPLINGS
KW  - HETERONUCLEAR NMR
KW  - AKAP SPECIFICITY
KW  - MAP2 EXPRESSION
KW  - LARGER PROTEINS
KW  - SH2 DOMAIN
UR  - https://www.jbc.org/article/S0021-9258(24)02052-0/fulltext
N2  - Isoforms of microtubule-associated protein 2 (MAP2) differ from their homolog Tau in the sequence and interactions of the N-terminal region. Binding of the N-terminal region of MAP2c (N-MAP2c) to the dimerization/docking domains of the regulatory subunit RIIa of cAMP-dependent protein kinase (RIIDD2) and to the Src-homology domain 2 (SH2) of growth factor receptor-bound protein 2 (Grb2) have been described long time ago. However, the structural features of the complexes remained unknown due to the disordered nature of MAP2. Here, we provide structural description of the complexes. We have solved solution structure of N-MAP2c in complex with RIIDD2, confirming formation of an amphiphilic a-helix of MAP2c upon binding, defining orientation of the ahelix in the complex and showing that its binding register differs from previous predictions. Using chemical shift mapping, we characterized the binding interface of SH2-Grb2 and rat MAP2c phosphorylated by the tyrosine kinase Fyn in their complex and proposed a model explaining differences between SH2-Grb2 complexes with rat MAP2c and phosphopeptides with a Grb2-specific sequence. The results provide the structural basis of a potential role of MAP2 in regulating cAMPdependent phosphorylation cascade via interactions with RIIDD2 and Ras signaling pathway via interactions with SH2
ER  -

BARTOŠÍK, Viktor; Jitka PLUCAROVÁ; Alice LANÍKOVÁ; Zuzana JANÁČKOVÁ; Petr PADRTA; Séverine JANSEN; Tobias GRUBER; Vojtěch VAŘEČKA; Stephan M FELLER and Lukáš ŽÍDEK. Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways. \textit{International Journal of Biological Chemistry}. AMSTERDAM: ANSInet, 2024, vol.~300, No~8, p.~1-22. ISSN~0021-9258. Available from: https://dx.doi.org/10.1016/j.jbc.2024.107551.

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