Protein 4.1, (Erythrocyte membrane protein band 4.1), is a
protein associated with the
cytoskeleton that in humans is encoded by the EPB41gene. Protein 4.1 is a major structural element of the
erythrocytemembrane 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.
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]
^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).
PMID10887144.{{
cite journal}}: CS1 maint: DOI inactive as of April 2024 (
link)
Conboy JG (1993). "Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells". Semin. Hematol. 30 (1): 58–73.
PMID8434260.
Tang TK, Leto TL, Marchesi VT, Benz EJ (1988). "Expression of Specific Isoforms of Protein 4.1 in Erythroid and Non-Erythroid Tissues". Molecular Biology of Hemopoiesis. Advances in Experimental Medicine and Biology. Vol. 241. pp. 81–95.
doi:
10.1007/978-1-4684-5571-7_12.
ISBN978-1-4684-5573-1.
PMID3223413.
Protein 4.1, (Erythrocyte membrane protein band 4.1), is a
protein associated with the
cytoskeleton that in humans is encoded by the EPB41gene. Protein 4.1 is a major structural element of the
erythrocytemembrane 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.
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]
^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).
PMID10887144.{{
cite journal}}: CS1 maint: DOI inactive as of April 2024 (
link)
Conboy JG (1993). "Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells". Semin. Hematol. 30 (1): 58–73.
PMID8434260.
Tang TK, Leto TL, Marchesi VT, Benz EJ (1988). "Expression of Specific Isoforms of Protein 4.1 in Erythroid and Non-Erythroid Tissues". Molecular Biology of Hemopoiesis. Advances in Experimental Medicine and Biology. Vol. 241. pp. 81–95.
doi:
10.1007/978-1-4684-5571-7_12.
ISBN978-1-4684-5573-1.
PMID3223413.