Protein 4.1

Last updated
EPB41
Protein EPB41 PDB 1gg3.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases EPB41 , erythrocyte membrane protein band 4.1, 4.1R, EL1, HE
External IDs OMIM: 130500 MGI: 95401 HomoloGene: 44324 GeneCards: EPB41
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001128606
NM_001128607
NM_183428

RefSeq (protein)

NP_001122078
NP_001122079
NP_906273

Location (UCSC) Chr 1: 28.89 – 29.12 Mb Chr 4: 131.92 – 132.08 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Protein 4.1, (Erythrocyte membrane protein band 4.1), is a protein associated with the cytoskeleton that in humans is encoded by the EPB41 gene. Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Protein 4.1 (80 kD) interacts with spectrin and short actin filaments to form the erythrocyte membrane skeleton. Mutations of spectrin and protein 4.1 are associated with elliptocytosis or spherocytosis and anemia of varying severity.

Clinical significance

A schematic diagram representing the relationships between cytoskeletal molecules as relevant to hereditary elliptocytosis. Cytoskeleton (Elliptocytosis).JPG
A schematic diagram representing the relationships between cytoskeletal molecules as relevant to hereditary elliptocytosis.

Elliptocytosis is a hematologic disorder characterized by elliptically shaped erythrocytes and a variable degree of hemolytic anemia. Inherited as an autosomal dominant, elliptocytosis results from mutation in any one of several genes encoding proteins of the red cell membrane skeleton. The form discussed here is the one found in the 1950s to be linked to Rh blood group and more recently shown to be caused by a defect in protein 4.1. 'Rh-unlinked' forms of elliptocytosis are caused by mutation in the alpha-spectrin gene (MIM 182860), the beta-spectrin gene (MIM 182870), or the band 3 gene (MIM 109270) [supplied by OMIM]. [5]

Interactions

Protein 4.1 has been shown to interact with:

See also

Related Research Articles

Glycophorin C plays a functionally important role in maintaining erythrocyte shape and regulating membrane material properties, possibly through its interaction with protein 4.1. Moreover, it has previously been shown that membranes deficient in protein 4.1 exhibit decreased content of glycophorin C. It is also an integral membrane protein of the erythrocyte and acts as the receptor for the Plasmodium falciparum protein PfEBP-2.

<span class="mw-page-title-main">Spectrin</span>

Spectrin is a cytoskeletal protein that lines the intracellular side of the plasma membrane in eukaryotic cells. Spectrin forms pentagonal or hexagonal arrangements, forming a scaffold and playing an important role in maintenance of plasma membrane integrity and cytoskeletal structure. The hexagonal arrangements are formed by tetramers of spectrin subunits associating with short actin filaments at either end of the tetramer. These short actin filaments act as junctional complexes allowing the formation of the hexagonal mesh. The protein is named spectrin since it was first isolated as a major protein component of human red blood cells which had been treated with mild detergents; the detergents lysed the cells and the hemoglobin and other cytoplasmic components were washed out. In the light microscope the basic shape of the red blood cell could still be seen as the spectrin-containing submembranous cytoskeleton preserved the shape of the cell in outline. This became known as a red blood cell "ghost" (spectre), and so the major protein of the ghost was named spectrin.

<span class="mw-page-title-main">Hereditary elliptocytosis</span> Medical condition

Hereditary elliptocytosis, also known as ovalocytosis, is an inherited blood disorder in which an abnormally large number of the person's red blood cells are elliptical rather than the typical biconcave disc shape. Such morphologically distinctive erythrocytes are sometimes referred to as elliptocytes or ovalocytes. It is one of many red-cell membrane defects. In its severe forms, this disorder predisposes to haemolytic anaemia. Although pathological in humans, elliptocytosis is normal in camelids.

<span class="mw-page-title-main">Band 3 anion transport protein</span> Mammalian protein found in Homo sapiens

Band 3 anion transport protein, also known as anion exchanger 1 (AE1) or band 3 or solute carrier family 4 member 1 (SLC4A1), is a protein that is encoded by the SLC4A1 gene in humans.

<span class="mw-page-title-main">Hereditary pyropoikilocytosis</span> Medical condition

Hereditary pyropoikilocytosis (HPP) is an autosomal recessive form of hemolytic anemia characterized by an abnormal sensitivity of red blood cells to heat and erythrocyte morphology similar to that seen in thermal burns or from prolonged exposure of a healthy patient's blood sample to high ambient temperatures. Patients with HPP tend to experience severe hemolysis and anemia in infancy that gradually improves, evolving toward typical elliptocytosis later in life. However, the hemolysis can lead to rapid sequestration and destruction of red cells. Splenectomy is curative when this occurs.

<span class="mw-page-title-main">Protein 4.2</span> Protein-coding gene in the species Homo sapiens

Erythrocyte membrane protein band 4.2 is a protein that in humans is encoded by the EPB42 gene. It is part of the red blood cell cytoskeleton.

<span class="mw-page-title-main">TPM1</span> Protein-coding gene in the species Homo sapiens

Tropomyosin alpha-1 chain is a protein that in humans is encoded by the TPM1 gene. This gene is a member of the tropomyosin (Tm) family of highly conserved, widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells.

<span class="mw-page-title-main">Spectrin, alpha 1</span> Protein-coding gene in the species Homo sapiens

Spectrin alpha chain, erythrocyte is a protein that in humans is encoded by the SPTA1 gene.

<span class="mw-page-title-main">SPTAN1</span> Protein-coding gene in the species Homo sapiens

Alpha II-spectrin, also known as Spectrin alpha chain, brain is a protein that in humans is encoded by the SPTAN1 gene. Alpha II-spectrin is expressed in a variety of tissues, and is highly expressed in cardiac muscle at Z-disc structures, costameres and at the sarcolemma membrane. Mutations in alpha II-spectrin have been associated with early infantile epileptic encephalopathy-5, and alpha II-spectrin may be a valuable biomarker for Guillain–Barré syndrome and infantile congenital heart disease.

<span class="mw-page-title-main">SPTB</span> Protein-coding gene in the species Homo sapiens

Spectrin beta chain, erythrocyte is a protein that in humans is encoded by the SPTB gene.

<span class="mw-page-title-main">Alpha-actinin-4</span> Protein-coding gene in the species Homo sapiens

Alpha-actinin-4 is a protein that in humans is encoded by the ACTN4 gene.

<span class="mw-page-title-main">SPTBN1</span> Protein-coding gene in the species Homo sapiens

Spectrin beta chain, brain 1 is a protein that in humans is encoded by the SPTBN1 gene.

<span class="mw-page-title-main">ADD2</span> Protein-coding gene in the species Homo sapiens

Beta-adducin is a protein that in humans is encoded by the ADD2 gene.

<span class="mw-page-title-main">EPB41L1</span> Protein-coding gene in the species Homo sapiens

Band 4.1-like protein 1 is a protein that in humans is encoded by the EPB41L1 gene.

<span class="mw-page-title-main">EPB41L2</span> Protein-coding gene in the species Homo sapiens

Band 4.1-like protein 2 is a protein that in humans is encoded by the EPB41L2 gene.

<span class="mw-page-title-main">ADD3</span> Protein-coding gene in the species Homo sapiens

Gamma-adducin is a protein that in humans is encoded by the ADD3 gene.

<span class="mw-page-title-main">SPTBN2</span> Protein-coding gene in the species Homo sapiens

Spectrin beta chain, brain 2 is a protein that in humans is encoded by the SPTBN2 gene.

<span class="mw-page-title-main">SPTBN4</span> Protein-coding gene in the species Homo sapiens

Spectrin, beta, non-erythrocytic 4, also known as SPTBN4, is a protein that in humans is encoded by the SPTBN4 gene.

<span class="mw-page-title-main">EPB49</span> Protein-coding gene in the species Homo sapiens

Dematin is a protein that in humans is encoded by the EPB49 gene.

<span class="mw-page-title-main">Ankyrin-1</span> Protein-coding gene in the species Homo sapiens

Ankyrin 1, also known as ANK-1, and erythrocyte ankyrin, is a protein that in humans is encoded by the ANK1 gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000159023 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028906 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "Entrez Gene: EPB41 erythrocyte membrane protein band 4.1 (elliptocytosis 1, RH-linked)".
  6. Hung LY, Tang CJ, Tang TK (October 2000). "Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) which is associated with the gamma-tubulin complex". Mol. Cell. Biol. 20 (20): 7813–25. doi:10.1128/mcb.20.20.7813-7825.2000. PMC   86375 . PMID   11003675.
  7. Hou CL, Tang Cj, Roffler SR, Tang TK (July 2000). "Protein 4.1R binding to eIF3-p44 suggests an interaction between the cytoskeletal network and the translation apparatus". Blood. 96 (2): 747–53. doi:10.1182/blood.V96.2.747.014k19_747_753 (inactive 2024-04-10). PMID   10887144.{{cite journal}}: CS1 maint: DOI inactive as of April 2024 (link)
  8. Mattagajasingh SN, Huang SC, Hartenstein JS, Snyder M, Marchesi VT, Benz EJ (April 1999). "A nonerythroid isoform of protein 4.1R interacts with the nuclear mitotic apparatus (NuMA) protein". J. Cell Biol. 145 (1): 29–43. doi:10.1083/jcb.145.1.29. PMC   2148212 . PMID   10189366.
  9. Mattagajasingh SN, Huang SC, Hartenstein JS, Benz EJ (September 2000). "Characterization of the interaction between protein 4.1R and ZO-2. A possible link between the tight junction and the actin cytoskeleton". J. Biol. Chem. 275 (39): 30573–85. doi: 10.1074/jbc.M004578200 . PMID   10874042.

Further reading