Literature DB >> 19269200

Protein 4.2: a complex linker.

Timothy J Satchwell1, Debbie K Shoemark, Richard B Sessions, Ashley M Toye.   

Abstract

The peripheral membrane protein, protein 4.2, is one of the most abundant protein components of the erythrocyte membrane. Protein 4.2 has an important role in red cell membrane structure, its absence due to natural mutations in humans or gene knockout in mice has a detrimental effect on membrane stability and results in hereditary spherocytosis. It is known to be a point of connection between the band 3 complex and the Rhesus protein complex, through its associations with band 3 and CD47 and also via interactions with the cytoskeletal protein ankyrin. Considering its relatively high abundance and importance in stability of the erythrocyte membrane, protein 4.2 has proved a somewhat neglected protein in recent years. In this review we will summarize our current understanding of protein 4.2, discuss its known interactions and describe the effects and implications of protein 4.2 deficiency. Based on protein 4.2's close homology with transglutaminase family proteins, we propose a new speculative "open" homology structure for protein 4.2 that may represent the active, membrane associated protein 4.2 molecule in red blood cells and also explain the dependence of protein 4.2 on band 3 binding for stability.

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Year:  2009        PMID: 19269200     DOI: 10.1016/j.bcmd.2009.01.005

Source DB:  PubMed          Journal:  Blood Cells Mol Dis        ISSN: 1079-9796            Impact factor:   3.039


  24 in total

1.  Compound heterozygosity for two novel mutations in the erythrocyte protein 4.2 gene causing spherocytosis in a Caucasian patient.

Authors:  Adrienne M Hammill; Mary A Risinger; Clinton H Joiner; Mehdi Keddache; Theodosia A Kalfa
Journal:  Br J Haematol       Date:  2011-01-31       Impact factor: 6.998

Review 2.  Transglutaminase 2: a molecular Swiss army knife.

Authors:  Soner Gundemir; Gozde Colak; Janusz Tucholski; Gail V W Johnson
Journal:  Biochim Biophys Acta       Date:  2011-10-10

3.  Analysis of the mobilities of band 3 populations associated with ankyrin protein and junctional complexes in intact murine erythrocytes.

Authors:  Gayani C Kodippili; Jeff Spector; Jacob Hale; Katie Giger; Michael R Hughes; Kelly M McNagny; Connie Birkenmeier; Luanne Peters; Ken Ritchie; Philip S Low
Journal:  J Biol Chem       Date:  2011-12-06       Impact factor: 5.157

Review 4.  The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.

Authors:  Anthony J Baines
Journal:  Protoplasma       Date:  2010-07-29       Impact factor: 3.356

5.  The carboxyterminal EF domain of erythroid alpha-spectrin is necessary for optimal spectrin-actin binding.

Authors:  Catherine Korsgren; Samuel E Lux
Journal:  Blood       Date:  2010-06-28       Impact factor: 22.113

6.  Investigating the key membrane protein changes during in vitro erythropoiesis of protein 4.2 (-) cells (mutations Chartres 1 and 2).

Authors:  Emile van den Akker; Timothy J Satchwell; Stephanie Pellegrin; Joanna F Flatt; Michel Maigre; Geoff Daniels; Jean Delaunay; Lesley J Bruce; Ashley M Toye
Journal:  Haematologica       Date:  2010-02-23       Impact factor: 9.941

7.  Identification of the components of a glycolytic enzyme metabolon on the human red blood cell membrane.

Authors:  Estela Puchulu-Campanella; Haiyan Chu; David J Anstee; Jacob A Galan; W Andy Tao; Philip S Low
Journal:  J Biol Chem       Date:  2012-11-13       Impact factor: 5.157

8.  The over-expression of aquaporin-1 alters erythroid gene expression in human erythroleukemia K562 cells.

Authors:  Min Wei; Rong Shi; Jun Zeng; Nisha Wang; Jueyu Zhou; Wenli Ma
Journal:  Tumour Biol       Date:  2014-09-25

9.  A novel complex, RUNX1-MYEF2, represses hematopoietic genes in erythroid cells.

Authors:  Boet van Riel; Tibor Pakozdi; Rutger Brouwer; Rui Monteiro; Kapil Tuladhar; Vedran Franke; Jan Christian Bryne; Ruud Jorna; Erik-Jan Rijkers; Wilfred van Ijcken; Charlotte Andrieu-Soler; Jeroen Demmers; Roger Patient; Eric Soler; Boris Lenhard; Frank Grosveld
Journal:  Mol Cell Biol       Date:  2012-07-16       Impact factor: 4.272

10.  Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid alpha-spectrin in a calcium- and calmodulin-dependent manner.

Authors:  Catherine Korsgren; Luanne L Peters; Samuel E Lux
Journal:  J Biol Chem       Date:  2009-12-11       Impact factor: 5.157

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