PuSH - Publication Server of Helmholtz Zentrum München

Bogusławska, D.M.* ; Machnicka, B.* ; Hryniewicz-Jankowska, A.* ; Czogalla, A.*

Spectrin and phospholipids - the current picture of their fascinating interplay.

Cell. Mol. Biol. Lett. 19, 158-179 (2014)
DOI Order publishers version
Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
The spectrin-based membrane skeleton is crucial for the mechanical stability and resilience of erythrocytes. It mainly contributes to membrane integrity, protein organization and trafficking. Two transmembrane protein macro-complexes that are linked together by spectrin tetramers play a crucial role in attaching the membrane skeleton to the cell membrane, but they are not exclusive. Considerable experimental data have shown that direct interactions between spectrin and membrane lipids are important for cell membrane cohesion. Spectrin is a multidomain, multifunctional protein with several distinctive structural regions, including lipid-binding sites within CH tandem domains, a PH domain, and triple helical segments, which are excellent examples of ligand specificity hidden in a regular repetitive structure, as recently shown for the ankyrin-sensitive lipid-binding domain of beta spectrin. In this review, we summarize the state of knowledge about interactions between spectrin and membrane lipids.
Additional Metrics?
Edit extra informations Login
Publication type Article: Journal article
Document type Review
ISSN (print) / ISBN 1425-8153
e-ISSN 1689-1392
Quellenangaben Volume: 19, Issue: 1, Pages: 158-179 Article Number: , Supplement: ,
Publisher Springer
Publishing Place Warsaw : Versita ; Berlin ; Heidelberg
Reviewing status Peer reviewed
Institute(s) Institute for Pancreatic Beta Cell Research (IPI)