Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences.
intrinsically disordered protein
microtubule associated protein
nuclear magnetic resonance
phosphorylation
tau
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
16 03 2019
16 03 2019
Historique:
received:
30
01
2019
revised:
09
03
2019
accepted:
13
03
2019
entrez:
20
3
2019
pubmed:
20
3
2019
medline:
23
8
2019
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 30884818
pii: biom9030105
doi: 10.3390/biom9030105
pmc: PMC6468450
pii:
doi:
Substances chimiques
Microtubule-Associated Proteins
0
tau Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
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