English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Structure and functions of microtubule associated proteins tau and MAP2c: Similarities and differences.

Melková, K., Zapletal, V., Narasimhan, S., Jansen, S., Hritz, J., Škrabana, R., et al. (2019). Structure and functions of microtubule associated proteins tau and MAP2c: Similarities and differences. Biomolecules, 9(3): 105. doi:10.3390/biom9030105.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0003-3553-4 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-3557-0
Genre: Journal Article

Files

show Files
hide Files
:
3034494.pdf (Publisher version), 683KB
Name:
3034494.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
:
3034494_Suppl.pdf (Supplementary material), 403KB
Name:
3034494_Suppl.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Melková, K., Author
Zapletal, V., Author
Narasimhan, S., Author
Jansen, S., Author
Hritz, J., Author
Škrabana, R., Author
Zweckstetter, M.1, Author              
Ringkjøbing-Jensen, M., Author
Blackledge, M., Author
Žídek, L., Author
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

Content

show
hide
Free keywords: microtubule associated protein; tau; intrinsically disordered protein; phosphorylation; nuclear magnetic resonance
 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.

Details

show
hide
Language(s): eng - English
 Dates: 2019-03-16
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.3390/biom9030105
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biomolecules
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: 32 Volume / Issue: 9 (3) Sequence Number: 105 Start / End Page: - Identifier: -