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@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 = {http://dx.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 and Lukáš ŽÍDEK. Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences. \textit{Biomolecules}. Basel, Switzerland: MDPI AG, 2019, vol.~9, No~3, p.~105-136. ISSN~2218-273X. Available from: https://dx.doi.org/10.3390/biom9030105.
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