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. Biomolecules. Basel, Switzerland: MDPI AG, 2019, vol. 9, No 3, p. 105-136. ISSN 2218-273X. doi:10.3390/biom9030105.
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Basic information
Original name Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences
Authors MELKOVÁ, Kateřina (203 Czech Republic, belonging to the institution), Vojtěch ZAPLETAL (203 Czech Republic, belonging to the institution), Subhash NARASIMHAN (356 India, belonging to the institution), Séverine JANSEN (250 France, belonging to the institution), Jozef HRITZ (703 Slovakia, belonging to the institution), R. SKRABANA (703 Slovakia), M. ZWECKSTETTER (276 Germany), M. RINGKJOBING JENSEN (250 France), M. BLACKLEDGE (250 France) and Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution).
Edition Biomolecules, Basel, Switzerland, MDPI AG, 2019, 2218-273X.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10608 Biochemistry and molecular biology
Country of publisher Switzerland
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 4.082
RIV identification code RIV/00216224:14740/19:00109608
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.3390/biom9030105
UT WoS 000464413600001
Keywords in English microtubule associated protein; tau; intrinsically disordered protein; phosphorylation; nuclear magnetic resonance
Tags rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 5/3/2020 09:45.
Abstract
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.
Links
LTC17078, research and development projectName: Studium interakcí domén přirozeně neuspořádaného proteinu MAP2c (microtubule- associated protein 2c) s jeho vazebnými partnery pomocí výpočetních metod a nukleární magnetické rezonance
Investor: Ministry of Education, Youth and Sports of the CR, INTER-EXCELLENCE, INTER-COST
PrintDisplayed: 9/12/2021 06:03