Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F19%3A00109608" target="_blank" >RIV/00216224:14740/19:00109608 - isvavai.cz</a>
Result on the web
<a href="https://www.mdpi.com/2218-273X/9/3/105" target="_blank" >https://www.mdpi.com/2218-273X/9/3/105</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/biom9030105" target="_blank" >10.3390/biom9030105</a>
Alternative languages
Result language
angličtina
Original language name
Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/LTC17078" target="_blank" >LTC17078: Study of domain interactions of intrinsically disordered protein MAP2c (Microtubule-Associated Protein 2c) with its binding partners via computational methods and nuclear magnetic resonance</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biomolecules
ISSN
2218-273X
e-ISSN
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Volume of the periodical
9
Issue of the periodical within the volume
3
Country of publishing house
CH - SWITZERLAND
Number of pages
32
Pages from-to
105
UT code for WoS article
000464413600001
EID of the result in the Scopus database
2-s2.0-85063275716