Spectrin and phospholipids - the current picture of their fascinating interplay

• Autorzy: Boguslawska D.M. , Machnicka B. , Hryniewicz-Jankowska A. , Czogalla A.
• Języki publikacji: EN

Abstrakty

EN

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.

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2014
• Tom: 19
• Numer: 1
• Opis fizyczny: p.158-179,fig.,ref.

Twórcy

autor

Boguslawska D.M.

• University of Zielona Gora, Faculty of Biological Sciences, Poland

autor

Machnicka B.

• University of Zielona Gora, Faculty of Biological Sciences, Poland

autor

Hryniewicz-Jankowska A.

• University of Wroclaw, Faculty of Biotechnology, Laboratory of Cytobiochemistry, F.Joliot-Curie 14A, 50-383 Wroclaw

autor

Czogalla A.

• University of Wroclaw, Faculty of Biotechnology, Laboratory of Cytobiochemistry, F.Joliot-Curie 14A, 50-383 Wroclaw
• Paul Langerhans Institute Dresden, Faculty of Medicine Carl Gustav Carus at the TU Dresden, Germany

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