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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • 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

  • 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