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Ezrin
Ezrin also known as cytovillin or villin-2 is a protein that in humans is encoded by the ''EZR'' gene. Structure The N-terminus of ezrin contains a FERM domain which is further subdivided into three subdomains. The C-terminus contains an ERM domain. Function The cytoplasmic peripheral protein encoded by this gene can be phosphorylated by protein- tyrosine kinase in microvilli and is a member of the ERM protein family. This protein serves as a linker between plasma membrane and actin cytoskeleton The cytoskeleton is a complex, dynamic network of interlinking protein filaments present in the cytoplasm of all cells, including those of bacteria and archaea. In eukaryotes, it extends from the cell nucleus to the cell membrane and is compos .... It plays a key role in cell surface structure adhesion, migration, and organization. The N-terminal domain (also called FERM domain) binds sodium-hydrogen exchanger regulatory factor ( NHERF) protein (involving long-range ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Moesin
Moesin is a protein that in humans is encoded by the ''MSN'' gene. Moesin (for membrane-organizing extension spike protein) is a member of the ERM protein family which includes ezrin and radixin. ERM proteins appear to function as cross-linkers between plasma membranes and actin-based cytoskeleton The cytoskeleton is a complex, dynamic network of interlinking protein filaments present in the cytoplasm of all cells, including those of bacteria and archaea. In eukaryotes, it extends from the cell nucleus to the cell membrane and is compos ...s. Moesin is localized to filopodia and other membranous protrusions that are important for cell–cell recognition and signaling and for cell movement. Moesin has FERM domain at N-terminal. Interactions Moesin has been shown to interact with: * CD43 * ICAM3 * Neutrophil cytosolic factor 1, * Neutrophil cytosolic factor 4 * VCAM-1 * EZR References Further reading * * * * * * * * * * * * * * * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ERM Protein Family
The ERM protein family consists of three closely related proteins, ezrin, radixin and moesin. The three paralogs, ezrin, radixin and moesin, are present in vertebrates, whereas other species have only one ERM gene. Therefore, in vertebrates these paralogs likely arose by gene duplication. ERM proteins are highly conserved throughout evolution. More than 75% identity is observed in the N-terminal and the C-terminal of vertebrates (ezrin, radixin, moesin), ''Drosophila'' (dmoesin) and '' C. elegans'' (ERM-1) homologs. Structure ERM molecules contain the following three domains: * N-terminal globular domain, also called FERM domain ( Band 4.1, ezrin, radixin, moesin). The FERM domain allows ERM proteins to interact with integral proteins of the plasma membrane, or scaffolding proteins localized beneath the plasma membrane. The FERM domain is composed of three subdomains (F1, F2, F3) that are arranged as a cloverleaf. * extended alpha-helical domain. * charged C-terminal domain. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
NHERF
Sodium-hydrogen antiporter 3 regulator 1 (SLC9A3R1) is a human protein. It is a regulator of Sodium-hydrogen antiporter 3 and is encoded by the gene ''SLC9A3R1''. It is also known as ERM Binding Protein 50 (EBP50) or Na+/H+ Exchanger Regulatory Factor (NHERF1). It is believed to interact via long-range allostery, involving significant protein dynamics. Mechanism Members of the ezrin (VIL2; MIM 123900)-radixin (RDX; MIM 179410)-moesin (MSN; MIM 309845) (ERM) protein family are highly concentrated in the apical aspect of polarized epithelial cells. These cells are studded with microvilli containing bundles of actin filaments, which must attach to the membrane to assemble and maintain the microvilli. The ERM proteins, together with merlin, the NF2 (MIM 607379) gene product, are thought to be linkers between integral membrane and cytoskeletal proteins, and they bind directly to actin in vitro. Actin cytoskeleton reorganization requires the activation of a sodium/hydrogen exchanger ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sodium-hydrogen Exchange Regulatory Cofactor 2
Sodium-hydrogen exchange regulatory cofactor NHE-RF2 (NHERF-2) also known as tyrosine kinase activator protein 1 (TKA-1) or SRY-interacting protein 1 (SIP-1) is a protein that in humans is encoded by the ''SLC9A3R2'' (solute carrier family 9 isoform A3 regulatory factor 2) gene. NHERF-2 is a scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. It is necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. In addition, it may also act as scaffold protein in the nucleus. Function This regulatory protein (factor) interacts with a sodium/hydrogen exchanger NHE3 ( SLC9A3) in the brush border membrane of the proximal tubule, small intestine, and colon that plays a major role in transepithelial sodium absorption. SLC9A3R2, as well as SLC9A3R1 and protein kinase A phosphorylation, may play a role in NHE3 regulation. Int ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PIK3R1
Phosphatidylinositol 3-kinase regulatory subunit alpha is an enzyme that in humans is encoded by the ''PIK3R1'' gene. Function Phosphatidylinositol 3-kinase phosphorylates the inositol ring of phosphatidylinositol at the 3-prime position. The enzyme comprises a 110 kD catalytic subunit and a regulatory subunit of either 85, 55, or 50 kD. The ''Pik3r1'' gene locus encodes the 85 kD regulatory subunit, as well as 55 and 50 kD regulatory subunits. It used to be thought that alternative splicing of this gene resulted in three transcript variants encoding different isoforms. In fact, it has since been shown that the 55 and 50kD subunits have their own promotors within the gene locus ''Pik3r1''. Phosphatidylinositol 3-kinase plays an important role in the metabolic actions of insulin, and a mutation in this gene has been associated with insulin resistance. Suppression specifically of the 85kD subunit in early murine embryoid body development results in a transient cell-cell adhe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Merlin (protein)
Merlin (also called neurofibromin 2 or schwannomin) is a cytoskeletal protein. In humans, it is a tumor suppressor protein involved in neurofibromatosis type II. Sequence data reveal its similarity to the ERM protein family. ''Merlin'' is an acronym for "Moesin-Ezrin-Radixin-like protein". Gene Human merlin is coded by the gene ''NF2'' in chromosome 22. Mouse merlin gene is located on chromosome 11 and rat merlin gene on chromosome 17. Fruit fly merlin gene (symbol ''Mer'') is located on chromosome 1 and shares 58% similarity to its human homologue. Other merlin-like genes are known from a wide range of animals, and the derivation of merlin is thought to be in early metazoa. Merlin is a member of the ERM family of proteins including ezrin, moesin, and radixin, which are in the protein 4.1 superfamily of proteins. Merlin is also known as ''schwannomin'', a name derived from the most common type of tumor in the NF2 patient phenotype, the schwannoma. Structure Vertebrate mer ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CD43
Leukosialin also known as sialophorin or CD43 (cluster of differentiation 43) is a transmembrane cell surface protein that in humans is encoded by the ''SPN'' (sialophorin) gene. Function Sialophorin (leukosialin) is a major sialoglycoprotein on the surface of human T lymphocytes, monocytes, granulocytes, and some B lymphocytes, which appears to be important for immune function and may be part of a physiologic ligand-receptor complex involved in T-cell activation. Clinical significance Defects in the CD43 molecule are associated with the development of Wiskott–Aldrich syndrome. It also appears in about 25% of intestinal MALTomas. Using immunohistochemistry, CD43 can be demonstrated in the paracortical T-cells of healthy lymph nodes and tonsils; it is also positive in a range of lymphoid and myeloid tumours. Although it is present in over 90% of T-cell lymphomas, it is generally less effective at demonstrating this condition than is CD3 antigen. However, it may be useful ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CD44
The CD44 antigen is a cell-surface glycoprotein involved in cell–cell interactions, cell adhesion and migration. In humans, the CD44 antigen is encoded by the ''CD44'' gene on chromosome 11. CD44 has been referred to as HCAM (homing cell adhesion molecule), Pgp-1 (phagocytic glycoprotein-1), Hermes antigen, lymphocyte homing receptor, ECM-III, and HUTCH-1. Tissue distribution and isoforms CD44 is expressed in a large number of mammalian cell types. The standard isoform, designated CD44s, comprising exons 1–5 and 16–20 is expressed in most cell types. CD44 splice variants containing variable exons are designated CD44v. Some epithelial cells also express a larger isoform (CD44E), which includes exons v8–10. Function CD44 participates in a wide variety of cellular functions including lymphocyte activation, recirculation and homing, hematopoiesis, and tumor metastasis. CD44 is a receptor for hyaluronic acid and internalizes metals bound to hyaluronic acid and can a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
FERM Domain
In molecular biology, the FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus in the majority of proteins in which it is found. Structure and function Ezrin, moesin, and radixin are highly related proteins (ERM protein family), but the other proteins in which the FERM domain is found do not share any region of similarity outside of this domain. ERM proteins are made of three domains, the FERM domain, a central helical domain and a C-terminal tail domain, which binds F-actin. The amino-acid sequence of the FERM domain is highly conserved among ERM proteins and is responsible for membrane association by direct binding to the cytoplasmic domain or tail ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fas Ligand
Fas ligand (FasL, also known as CD95L or Apo-1L) is a type-II transmembrane protein in the tumor necrosis factor (TNF) superfamily. It binds to the Fas receptor (CD95) to induce apoptosis, and also activates non-apoptotic pathways such as NF-κB and Mitogen-activated protein kinase, MAPK. FasL exists in membrane-bound and soluble forms, and is primarily expressed by cytotoxic T lymphocytes and natural killer cells. It plays a critical role in immune regulation, immune privilege, cancer, autoimmunity, and transplantation. The expression and function of FasL are tightly regulated to maintain Homeostasis, immune homeostasis. Structure Fas ligand operates as a type-II transmembrane protein through its membership in the tumor necrosis factor (TNF) superfamily. It operates under its official names FasL and CD95L or Apo-1L. With 281 amino acids the protein forms three identifiable structural components by including an intracellular N-terminal domain then follows with one transmembrane ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ICAM2
Intercellular adhesion molecule 2 (ICAM2), also known as CD102 (Cluster of Differentiation 102), is a human gene, and the protein resulting from it. Protein structure The protein encoded by this gene is a member of the intercellular adhesion molecule (ICAM) family. All ICAM proteins are type I transmembrane glycoproteins, contain 2–9 immunoglobulin-like C2-type domains, and bind to the leukocyte adhesion LFA-1 protein. Protein functions ICAM-2 molecules regulate spermatid adhesion on Sertoli cell on the apical side of the blood-testis barrier (towards the lumen), thus playing a major role in spermatogenesis. This protein may also play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance. Interactions ICAM2 has been shown to interact w ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |