SPECTRIN AND PHOSPHOLIPIDS - THE CURRENT PICTURE OF THEIR FASCINATING INTERPLAY

被引：24

作者：

Boguslawska, Dzamila M. ^{[1
]}

Machnicka, Beata ^{[1
]}

Hryniewicz-Jankowska, Anita ^{[2
]}

Czogalla, Aleksander ^{[2
,3
]}

机构：

[1] Univ Zielona Gora, Fac Biol Sci, Zielona Gora, Poland

[2] Univ Wroclaw, Fac Biotechnol, PL-50383 Wroclaw, Poland

[3] Tech Univ Dresden, Fac Med Carl Gustav Carus, Paul Langerhans Inst Dresden, Dresden, Germany

来源：

CELLULAR & MOLECULAR BIOLOGY LETTERS | 2014年 / 19卷 / 01期

关键词：

Spectrin-phospholipid interactions; Spectrin repeats; Spectrin tetramers; Ankyrin; Erythrocytes; Actin-binding domain; Pleckstrin homology domain; Dystrophin; Lipid bilayer; Membrane skeleton; RED-CELL MEMBRANE; ERYTHROID BETA-SPECTRIN; ALPHA-II-SPECTRIN; PHOSPHATIDYLSERINE BINDING-SITES; PLECKSTRIN HOMOLOGY DOMAINS; DYSTROPHIN ROD DOMAIN; CRYSTAL-STRUCTURE; ANKYRIN-BINDING; LIPID-BINDING; CALCIUM-BINDING;

D O I：

10.2478/s11658-014-0185-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：158 / 179

页数：22

共 136 条

[1] Disorders of red cell membrane [J].

An, Xiuli ;

Mohandas, Narla .

BRITISH JOURNAL OF HAEMATOLOGY, 2008, 141 (03) :367-375

[2] Identification and functional characterization of protein 4.1R and actin-binding sites in erythrocyte β spectrin:: Regulation of the interactions by phosphatidylinositol-4,5-bisphosphate [J].

An, XL ;

Debnath, G ;

Guo, XH ;

Liu, SW ;

Lux, SE ;

Baines, A ;

Gratzer, W ;

Mohandas, N .

BIOCHEMISTRY, 2005, 44 (31) :10681-10688

[3] Phospholipid binding by proteins of the spectrin family: a comparative study [J].

An, XL ;

Guo, XH ;

Gratzer, W ;

Mohandas, N .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2005, 327 (03) :794-800

[4] Phosphatidylserine binding sites in red cell spectrin [J].

An, XL ;

Guo, XH ;

Wu, Y ;

Mohandas, N .

BLOOD CELLS MOLECULES AND DISEASES, 2004, 32 (03) :430-432

[5] Phosphatidylserine binding sites in erythroid spectrin: Location and implications for membrane stability [J].

An, XL ;

Guo, XH ;

Sum, H ;

Morrow, J ;

Gratzer, W ;

Mohandas, N .

BIOCHEMISTRY, 2004, 43 (02) :310-315

[6] The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life [J].

Baines, Anthony J. .

PROTOPLASMA, 2010, 244 (1-4) :99-131

[7]

BandorowiczPikula J, 1996, MOL MEMBR BIOL, V13, P241

[8] Hereditary red cell membrane defects: diagnostic and clinical aspects [J].

Barcellini, Wilma ;

Bianchi, Paola ;

Fermo, Elisa ;

Imperiali, Francesca G. ;

Marcello, Anna P. ;

Vercellati, Cristina ;

Zaninoni, Anna ;

Zanella, Alberto .

BLOOD TRANSFUSION, 2011, 9 (03) :274-277

[9] Spectrin and ankyrin-based pathways: Metazoan inventions for integrating cells into tissues [J].

Bennett, V ;

Baines, AJ .

PHYSIOLOGICAL REVIEWS, 2001, 81 (03) :1353-1392

[10]

BENNETT V, 1979, J BIOL CHEM, V254, P2533

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