Structure and Functions of Microtubule Associated Proteins Tau
and MAP2c: Similarities and Differences

J 2019

Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences

MELKOVÁ, Kateřina; Vojtěch ZAPLETAL; Subhash NARASIMHAN; Séverine JANSEN; Jozef HRITZ et. al.

Základní údaje

Originální název

Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences

Autoři

MELKOVÁ, Kateřina; Vojtěch ZAPLETAL; Subhash NARASIMHAN; Séverine JANSEN; Jozef HRITZ; R. SKRABANA; M. ZWECKSTETTER; M. RINGKJOBING JENSEN; M. BLACKLEDGE a Lukáš ŽÍDEK

Vydání

Biomolecules, Basel, Switzerland, MDPI AG, 2019, 2218-273X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Švýcarsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.082

Kód RIV

RIV/00216224:14740/19:00109608

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.3390/biom9030105

UT WoS

000464413600001

EID Scopus

2-s2.0-85063275716

Klíčová slova anglicky

microtubule associated protein; tau; intrinsically disordered protein; phosphorylation; nuclear magnetic resonance

Štítky

143160, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 5. 3. 2020 09:45, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

The stability and dynamics of cytoskeleton in brain nerve cells are regulated by microtubule associated proteins (MAPs), tau and MAP2. Both proteins are intrinsically disordered and involved in multiple molecular interactions important for normal physiology and pathology of chronic neurodegenerative diseases. Nuclear magnetic resonance and cryo-electron microscopy recently revealed propensities of MAPs to form transient local structures and long-range contacts in the free state, and conformations adopted in complexes with microtubules and filamentous actin, as well as in pathological aggregates. In this paper, we compare the longest, 441-residue brain isoform of tau (tau40), and a 467-residue isoform of MAP2, known as MAP2c. For both molecules, we present transient structural motifs revealed by conformational analysis of experimental data obtained for free soluble forms of the proteins. We show that many of the short sequence motifs that exhibit transient structural features are linked to functional properties, manifested by specific interactions. The transient structural motifs can be therefore classified as molecular recognition elements of tau40 and MAP2c. Their interactions are further regulated by post-translational modifications, in particular phosphorylation. The structure-function analysis also explains differences between biological activities of tau40 and MAP2c.

Návaznosti

LTC17078, projekt VaV

Název: Studium interakcí domén přirozeně neuspořádaného proteinu MAP2c (microtubule- associated protein 2c) s jeho vazebnými partnery pomocí výpočetních metod a nukleární magnetické rezonance

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Studium interakcí domén přirozeně neuspořádaného proteinu MAP2c (microtubule-associated protein 2c) s jeho vazebnými partnery pomocí výpočetních metod a nukleární magnetické rezonance, INTER-COST

Citovat

MELKOVÁ, Kateřina; Vojtěch ZAPLETAL; Subhash NARASIMHAN; Séverine JANSEN; Jozef HRITZ; R. SKRABANA; M. ZWECKSTETTER; M. RINGKJOBING JENSEN; M. BLACKLEDGE a Lukáš ŽÍDEK. Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences. Biomolecules. Basel, Switzerland: MDPI AG, 2019, roč. 9, č. 3, s. 105-136. ISSN 2218-273X. Dostupné z: https://doi.org/10.3390/biom9030105.

@article{1529019,
   author = {Melková, Kateřina and Zapletal, Vojtěch and Narasimhan, Subhash and Jansen, Séverine and Hritz, Jozef and Skrabana, R. and Zweckstetter, M. and Ringkjobing Jensen, M. and Blackledge, M. and Žídek, Lukáš},
   article_location = {Basel, Switzerland},
   article_number = {3},
   doi = {https://doi.org/10.3390/biom9030105},
   keywords = {microtubule associated protein; tau; intrinsically disordered protein; phosphorylation; nuclear magnetic resonance},
   language = {eng},
   issn = {2218-273X},
   journal = {Biomolecules},
   title = {Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences},
   url = {https://www.mdpi.com/2218-273X/9/3/105},
   volume = {9},
   year = {2019}
}

TY  - JOUR
ID  - 1529019
AU  - Melková, Kateřina - Zapletal, Vojtěch - Narasimhan, Subhash - Jansen, Séverine - Hritz, Jozef - Skrabana, R. - Zweckstetter, M. - Ringkjobing Jensen, M. - Blackledge, M. - Žídek, Lukáš
PY  - 2019
TI  - Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences
JF  - Biomolecules
VL  - 9
IS  - 3
SP  - 105
EP  - 105
PB  - MDPI AG
SN  - 2218273X
KW  - microtubule associated protein
KW  - tau
KW  - intrinsically disordered protein
KW  - phosphorylation
KW  - nuclear magnetic resonance
UR  - https://www.mdpi.com/2218-273X/9/3/105
L2  - https://www.mdpi.com/2218-273X/9/3/105
N2  - The stability and dynamics of cytoskeleton in brain nerve cells are regulated by microtubule associated proteins (MAPs), tau and MAP2. Both proteins are intrinsically disordered and involved in multiple molecular interactions important for normal physiology and pathology of chronic neurodegenerative diseases. Nuclear magnetic resonance and cryo-electron microscopy recently revealed propensities of MAPs to form transient local structures and long-range contacts in the free state, and conformations adopted in complexes with microtubules and filamentous actin, as well as in pathological aggregates. In this paper, we compare the longest, 441-residue brain isoform of tau (tau40), and a 467-residue isoform of MAP2, known as MAP2c. For both molecules, we present transient structural motifs revealed by conformational analysis of experimental data obtained for free soluble forms of the proteins. We show that many of the short sequence motifs that exhibit transient structural features are linked to functional properties, manifested by specific interactions. The transient structural motifs can be therefore classified as molecular recognition elements of tau40 and MAP2c. Their interactions are further regulated by post-translational modifications, in particular phosphorylation. The structure-function analysis also explains differences between biological activities of tau40 and MAP2c.
ER  -

MELKOVÁ, Kateřina; Vojtěch ZAPLETAL; Subhash NARASIMHAN; Séverine JANSEN; Jozef HRITZ; R. SKRABANA; M. ZWECKSTETTER; M. RINGKJOBING JENSEN; M. BLACKLEDGE a Lukáš ŽÍDEK. Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences. \textit{Biomolecules}. Basel, Switzerland: MDPI AG, 2019, roč.~9, č.~3, s.~105-136. ISSN~2218-273X. Dostupné z: https://doi.org/10.3390/biom9030105.

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