Detail
Článek
Článek online
FT
Medvik - BMČ
  • Je něco špatně v tomto záznamu ?

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

K. Melková, V. Zapletal, S. Narasimhan, S. Jansen, J. Hritz, R. Škrabana, M. Zweckstetter, M. Ringkjøbing Jensen, M. Blackledge, L. Žídek,

. 2019 ; 9 (3) : . [pub] 20190316

Jazyk angličtina Země Švýcarsko

Typ dokumentu časopisecké články, práce podpořená grantem, přehledy

Perzistentní odkaz   https://www.medvik.cz/link/bmc19034704

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.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc19034704
003      
CZ-PrNML
005      
20191011085102.0
007      
ta
008      
191007s2019 sz f 000 0|eng||
009      
AR
024    7_
$a 10.3390/biom9030105 $2 doi
035    __
$a (PubMed)30884818
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a sz
100    1_
$a Melková, Kateřina $u Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. katerina.melkova@ceitec.muni.cz. Faculty of Science, National Centre for Biomolecular Research, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. katerina.melkova@ceitec.muni.cz.
245    10
$a Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences / $c K. Melková, V. Zapletal, S. Narasimhan, S. Jansen, J. Hritz, R. Škrabana, M. Zweckstetter, M. Ringkjøbing Jensen, M. Blackledge, L. Žídek,
520    9_
$a 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.
650    _2
$a zvířata $7 D000818
650    _2
$a lidé $7 D006801
650    _2
$a proteiny asociované s mikrotubuly $x chemie $x metabolismus $7 D008869
650    _2
$a mikrotubuly $x chemie $x metabolismus $7 D008870
650    _2
$a proteiny tau $x chemie $x metabolismus $7 D016875
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
655    _2
$a přehledy $7 D016454
700    1_
$a Zapletal, Vojtěch $u Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. vojtech.zapletal@ceitec.muni.cz. Faculty of Science, National Centre for Biomolecular Research, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. vojtech.zapletal@ceitec.muni.cz.
700    1_
$a Narasimhan, Subhash $u Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. subhash.narasimhan@ceitec.muni.cz.
700    1_
$a Jansen, Séverine $u Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. severine@chemi.muni.cz.
700    1_
$a Hritz, Jozef $u Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. jozef.hritz@ceitec.muni.cz.
700    1_
$a Škrabana, Rostislav $u Institute of Neuroimmunology, Slovak Academy of Sciences, Dúbravská cesta 9, 845 10 Bratislava, Slovakia. rostislav.skrabana@savba.sk. Axon Neuroscience R&D Services SE, Dvořákovo nábrežie 10, 811 02 Bratislava, Slovakia. rostislav.skrabana@savba.sk.
700    1_
$a Zweckstetter, Markus $u German Center for Neurodegenerative Diseases (DZNE), Von-Siebold-Str. 3a, 37075 Göttingen, Germany. Markus.Zweckstetter@dzne.de. Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany. Markus.Zweckstetter@dzne.de.
700    1_
$a Ringkjøbing Jensen, Malene $u University Grenoble Alps, CEA, CNRS, 38000 Grenoble, France. malene.ringkjobing-jensen@ibs.fr.
700    1_
$a Blackledge, Martin $u University Grenoble Alps, CEA, CNRS, 38000 Grenoble, France. martin.blackledge@ibs.fr.
700    1_
$a Žídek, Lukáš $u Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. lzidek@chemi.muni.cz. Faculty of Science, National Centre for Biomolecular Research, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. lzidek@chemi.muni.cz.
773    0_
$w MED00188737 $t Biomolecules $x 2218-273X $g Roč. 9, č. 3 (2019)
856    41
$u https://pubmed.ncbi.nlm.nih.gov/30884818 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20191007 $b ABA008
991    __
$a 20191011085522 $b ABA008
999    __
$a ok $b bmc $g 1451364 $s 1073254
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2019 $b 9 $c 3 $e 20190316 $i 2218-273X $m Biomolecules $n Biomolecules $x MED00188737
LZP    __
$a Pubmed-20191007

Najít záznam

Citační ukazatele

Nahrávání dat ...

Možnosti archivace

Nahrávání dat ...