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.

Základní údaje

Originální název

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

Autoři

BARTOŠÍK, Viktor; Jitka PLUCAROVÁ; Alice LANÍKOVÁ; Zuzana JANÁČKOVÁ; Petr PADRTA; Séverine JANSEN; Tobias GRUBER; Vojtěch VAŘEČKA ; Stephan M FELLER a Lukáš ŽÍDEK

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.900

Kód RIV

RIV/00216224:14740/24:00138072

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.1016/j.jbc.2024.107551

UT WoS

001365739800001

EID Scopus

2-s2.0-85200983503

Klíčová slova anglicky

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

Štítky

14313010, 143160, CF BIC, CF NMR, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 3. 6. 2025 12:29, Mgr. Eva Dubská

Anotace

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

Návaznosti

EF18_046/0015974, projekt VaV

Název: Modernizace České infrastruktury pro integrativní strukturní biologii

GA20-12669S, projekt VaV

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

Investor: Grantová agentura ČR, Interactions defining physiological functions of Microtubule Associated Protein 2c at atomic resolution

MUNI/A/1641/2023, interní kód MU

Název: Struktura a dynamika biopolymerů

Investor: Masarykova univerzita, Struktura a dynamika biopolymerů

90242, velká výzkumná infrastruktura

Název: CIISB III

Citovat

BARTOŠÍK, Viktor; Jitka PLUCAROVÁ; Alice LANÍKOVÁ; Zuzana JANÁČKOVÁ; Petr PADRTA; Séverine JANSEN; Tobias GRUBER; Vojtěch VAŘEČKA; Stephan M FELLER a 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, roč. 300, č. 8, s. 1-22. ISSN 0021-9258. Dostupné z: https://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 = {https://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 a 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, roč.~300, č.~8, s.~1-22. ISSN~0021-9258. Dostupné z: https://doi.org/10.1016/j.jbc.2024.107551.

Přehled o publikaci