Interaction between protein 4.1R and spectrin heterodimers

被引：5

作者：

Zhang, Dao-Qiang ^{[1
]}

Wang, Yun-Peng ^{[1
]}

Wang, Wen-Hu ^{[1
]}

Sui, Xiu-Mei ^{[1
]}

Jiang, Jun-Qiang ^{[1
]}

Jiang, Xiao-Mei ^{[1
]}

Xu, Zu-Shan ^{[1
]}

Liu, Yan-Guang ^{[1
]}

机构：

[1] Wendeng Cent Hosp, Weifang Med Coll, Weihai 264400, Shandong, Peoples R China

来源：

MOLECULAR MEDICINE REPORTS | 2011年 / 4卷 / 04期

关键词：

protein; 4.1R; spectrin; binding; red blood cells; membrane; ERYTHROID ALPHA-SPECTRIN; BLOOD-CELL MEMBRANE; HEREDITARY ELLIPTOCYTOSIS; HEMOLYTIC-ANEMIAS; ACTIN-BINDING; DOMAIN; DEFICIENCY; MUTATIONS; STABILITY; COMPLEX;

D O I：

10.3892/mmr.2011.470

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

Defects or deficiencies in red cell membrane skeletal proteins often undermine the integrity and stability of the plasma membrane, and consequently cause hereditary hemolytic anemias. Genetic and biochemical studies have revealed a complicated picture of the organization of the membrane skeleton, within which alpha-/beta-spectrin heterodimers form a protein lattice. By stabilizing the red cell membrane skeleton, the erythroid protein 4.1R greatly contributes to connecting and regulating the interaction among spectrins, actin filaments and integral proteins on the plasma membrane. In this study, we demonstrated the direct interaction between 4.1R and alpha-/beta-spectrin. The results provide novel insights into the stoichiometry of 4.1R with spectrin, and demonstrate for the first time that the binding ratio of 4.1R to spectrin heterodimers is approximately 5.

引用

页码：651 / 654

页数：4

共 24 条

[1] Disorders of red cell membrane
An, Xiuli
Mohandas, Narla
[J]. 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
An, XL
Debnath, G
Guo, XH
Liu, SW
Lux, SE
Baines, A
Gratzer, W
Mohandas, N
[J]. BIOCHEMISTRY, 2005, 44 (31) : 10681 - 10688
[3] The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life
Baines, Anthony J.
[J]. PROTOPLASMA, 2010, 244 (1-4) : 99 - 131
[4] Spectrin and ankyrin-based pathways: Metazoan inventions for integrating cells into tissues
Bennett, V
Baines, AJ
[J]. PHYSIOLOGICAL REVIEWS, 2001, 81 (03) : 1353 - 1392
[5] Hereditary haemolytic anaemias: unexpected sequelae of mutations in the genes for erythroid membrane skeletal proteins
Birkenmeier, CS
Barker, JE
[J]. JOURNAL OF PATHOLOGY, 2004, 204 (04) : 450 - 459
[6] MOLECULAR-BASIS OF HEREDITARY ELLIPTOCYTOSIS DUE TO PROTEIN-4.1 DEFICIENCY
CONBOY, J
MOHANDAS, N
TCHERNIA, G
KAN, YW
[J]. NEW ENGLAND JOURNAL OF MEDICINE, 1986, 315 (11) : 680 - 685
[7] STRUCTURAL DOMAIN MAPPING AND PHOSPHORYLATION OF HUMAN ERYTHROCYTE PALLIDIN (BAND-4.2)
DOTIMAS, E
SPEICHER, DW
GUPTAROY, B
COHEN, CM
[J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1993, 1148 (01) : 19 - 29
[8] The prototypical 4.1R-10-kDa domain and the 4.1G-10-kDa paralog mediate fodrin-actin complex formation
Kontrogianni-Konstantopoulos, A
Frye, CS
Benz, EJ
Huang, SC
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (23) : 20679 - 20687
[9] The carboxyterminal EF domain of erythroid α-spectrin is necessary for optimal spectrin-actin binding
Korsgren, Catherine
Lux, Samuel E.
[J]. BLOOD, 2010, 116 (14) : 2600 - 2607
[10] Protein 4.2 Binds to the Carboxyl-terminal EF-hands of Erythroid α-Spectrin in a Calcium- and Calmodulin-dependent Manner
Korsgren, Catherine
Peters, Luanne L.
Lux, Samuel E.
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2010, 285 (07) : 4757 - 4770

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