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Nectin-4
Nectins and Nectin-like molecules (Necl) are families of cellular adhesion molecules involved in Ca2+-independent cellular adhesion. Nectins are ubiquitously expressed and have adhesive roles in a wide range of tissues such as the adherens junction of epithelia or the chemical synapse of the neuronal tissue. Diversity So far four nectins have been identified in humans, namely nectin-1, nectin-2, nectin-3 and nectin-4. These four family members have also been found in most other well studied mammals. Also, five Necls have been identified, these are: Necl-1, Necl-2, Necl-3, Necl-4 and Necl-5. Structure All nectins and all Necls share the same overall structure defined by three extra cellular immunoglobulin domains, a single transmembrane helix and an intracellular domain. For all nectins the intracellular domain can bind a scaffold protein named afadin (the product of the MLLT4 gene). All nectins and Necls can form homo-cis dimers, meaning a dimer of two alike molecules o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nectin-4
Nectins and Nectin-like molecules (Necl) are families of cellular adhesion molecules involved in Ca2+-independent cellular adhesion. Nectins are ubiquitously expressed and have adhesive roles in a wide range of tissues such as the adherens junction of epithelia or the chemical synapse of the neuronal tissue. Diversity So far four nectins have been identified in humans, namely nectin-1, nectin-2, nectin-3 and nectin-4. These four family members have also been found in most other well studied mammals. Also, five Necls have been identified, these are: Necl-1, Necl-2, Necl-3, Necl-4 and Necl-5. Structure All nectins and all Necls share the same overall structure defined by three extra cellular immunoglobulin domains, a single transmembrane helix and an intracellular domain. For all nectins the intracellular domain can bind a scaffold protein named afadin (the product of the MLLT4 gene). All nectins and Necls can form homo-cis dimers, meaning a dimer of two alike molecules o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nectin-4
Nectins and Nectin-like molecules (Necl) are families of cellular adhesion molecules involved in Ca2+-independent cellular adhesion. Nectins are ubiquitously expressed and have adhesive roles in a wide range of tissues such as the adherens junction of epithelia or the chemical synapse of the neuronal tissue. Diversity So far four nectins have been identified in humans, namely nectin-1, nectin-2, nectin-3 and nectin-4. These four family members have also been found in most other well studied mammals. Also, five Necls have been identified, these are: Necl-1, Necl-2, Necl-3, Necl-4 and Necl-5. Structure All nectins and all Necls share the same overall structure defined by three extra cellular immunoglobulin domains, a single transmembrane helix and an intracellular domain. For all nectins the intracellular domain can bind a scaffold protein named afadin (the product of the MLLT4 gene). All nectins and Necls can form homo-cis dimers, meaning a dimer of two alike molecules o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enfortumab Vedotin
Enfortumab vedotin, sold under the brand name Padcev, is an antibody-drug conjugate used for the treatment of urothelial cancer. It is a nectin-4-directed antibody and microtubule inhibitor conjugate. Enfortumab refers to the monoclonal antibody part, and vedotin refers to the payload drug (MMAE) and the linker. The most common side effects include fatigue, peripheral neuropathy (nerve damage resulting in tingling or numbness), decreased appetite, rash, alopecia (hair loss), nausea, altered taste, diarrhea, dry eye, pruritus (itching) and dry skin. The fully humanized antibody was created by scientists at Agensys (part of Astellas) using Xenomice from Amgen; the linker technology holding the antibody and the toxin together was provided by and licensed from Seattle Genetics. The U.S. Food and Drug Administration (FDA) considers it to be a first-in-class medication. Medical uses Enfortumab vedotin is indicated for the treatment of adults with locally advanced (when cancer has ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CD155
CD155 (cluster of differentiation 155) also known as the poliovirus receptor is a protein that in humans is encoded by the ''PVR'' gene. Function CD155 is a Type I transmembrane glycoprotein in the immunoglobulin superfamily. Commonly known as ''Poliovirus Receptor'' (PVR) due to its involvement in the cellular poliovirus infection in primates, CD155's normal cellular function is in the establishment of intercellular adherens junctions between epithelial cells. The role of CD155 in the immune system is unclear, though it may be involved in intestinal humoral immunity, humoral immune responses. Subsequent data has also suggested that CD155 may also be used to positively select MHC restriction, MHC-independent T cells in the thymus. The external domain mediates cell attachment to the extracellular matrix molecule vitronectin, while its intracellular domain interacts with the dynein light chain Tctex-1/DYNLT1. The gene is specific to the primate lineage, and serves as a cellular r ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lung Cancer 1
The lungs are the primary organs of the respiratory system in humans and most other animals, including some snails and a small number of fish. In mammals and most other vertebrates, two lungs are located near the backbone on either side of the heart. Their function in the respiratory system is to extract oxygen from the air and transfer it into the bloodstream, and to release carbon dioxide from the bloodstream into the atmosphere, in a process of gas exchange. Respiration is driven by different muscular systems in different species. Mammals, reptiles and birds use their different muscles to support and foster breathing. In earlier tetrapods, air was driven into the lungs by the pharyngeal muscles via buccal pumping, a mechanism still seen in amphibians. In humans, the main muscle of respiration that drives breathing is the diaphragm. The lungs also provide airflow that makes vocal sounds including human speech possible. Humans have two lungs, one on the left and one on the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PVRL3
Nectin-3, also known as nectin cell adhesion molecule 3, is a protein that in humans is encoded by the ''NECTIN3'' gene. Nectin-3 belongs to the family of immunoglobulin(Ig)-like cellular adhesion molecules involved in Ca2+-independent cellular adhesion in several tissues during the development and was firstly isolated at the turn of 20th and 21st century. Structure and localization Nectin-3 has three splicing variants, nectin-3α, which is the biggest one, nectin-3β and the smallest variant nectin-3γ. Nectin-3α (same as the other splicing variants) is abundately expressed in testis, on slightly level it is also expressed in heart, brain, liver or kidney. It has been also proved that nectin-3α is together with nectin-2 localize at the junctional complex regions in small intestina absorptive epitelia. Nectin-3γ is also detectable in lung, liver and kidney. Nectin-3 is expressed not only on epithelial cells as another nectins, but there was shown that, as the only membe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PVRL2
Poliovirus receptor-related 2 (PVRL2), also known as nectin-2 and CD112 (formerly herpesvirus entry mediator B, HVEB), is a human plasma membrane glycoprotein. Function This gene encodes a single-pass type I membrane glycoprotein with two Ig-like C2-type domains and an Ig-like V-type domain. This protein is one of the plasma membrane components of adherens junctions. It also serves as an entry for certain mutant strains of herpes simplex virus and pseudorabies virus, and it is involved in cell to cell spreading of these viruses. Variations in this gene have been associated with differences in the severity of multiple sclerosis. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. See also * Cluster of differentiation The cluster of differentiation (also known as cluster of designation or classification determinant and often abbreviated as CD) is a protocol used for the identification and investigation of cell surface molecules p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PVRL1
Poliovirus receptor-related 1 (PVRL1), also known as nectin-1 and CD111 (formerly herpesvirus entry mediator C, HVEC) is a human protein of the immunoglobulin superfamily (IgSF), also considered a member of the nectins. It is a membrane protein with three extracellular immunoglobulin domains, a single transmembrane helix and a cytoplasmic tail. The protein can mediate Ca2+-independent cellular adhesion further characterizing it as IgSF cell adhesion molecule (IgSF CAM). Function PVRL1 is an adhesion molecule found in a wide range of tissues where it localizes in various junctions such as the adherens junction of epithelial tissue or the chemical synapse of neurons. The cytoplasmic tail of PVRL1 can bind the protein afadin which is a scaffolding protein that binds actin. In the chemical synapse PVRL1 interacts with PVRL3 (nectin-3) and both proteins can be found in neuronal tissue already in early stages of brain development as well as in aging brains. The two proteins have b ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cadherin
Cadherins (named for "calcium-dependent adhesion") are a type of cell adhesion molecule (CAM) that is important in the formation of adherens junctions to allow cells to adhere to each other . Cadherins are a class of type-1 transmembrane proteins, and they are dependent on calcium (Ca2+) ions to function, hence their name. Cell-cell adhesion is mediated by extracellular cadherin domains, whereas the intracellular cytoplasmic tail associates with numerous adaptors and signaling proteins, collectively referred to as the cadherin adhesome. The cadherin family is essential in maintaining the cell-cell contact and regulating cytoskeletal complexes. The cadherin superfamily includes cadherins, protocadherins, desmogleins, desmocollins, and more. In structure, they share ''cadherin repeats'', which are the extracellular Ca2+-binding domains. There are multiple classes of cadherin molecules, each designated with a prefix (in general, noting the types of tissue with which it is associated). ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
MLLT4
Afadin is a protein that in humans is encoded by the ''AFDN'' gene. Function Afadin is a Ras (see HRAS; MIM 190020) target that regulates cell–cell adhesions downstream of Ras activation. It is fused with MLL (MIM 159555) in leukemias caused by t(6;11) translocations (Taya et al., 1998). upplied by OMIMref name="entrez"> Interactions Afadin has been shown to interact with: * BCR gene, * EPHB3, * F11 receptor, * HRAS and * LMO2, * PVRL1, * PVRL3, * Profilin 1, * RAP1A, * RAP1GAP, * SORBS1, * SSX2IP, * Tight junction protein 1 Zonula occludens-1 ZO-1, also known as Tight junction protein-1 is a 220-kD peripheral membrane protein that is encoded by the ''TJP1'' gene in humans. It belongs to the family of ''zonula occludens proteins'' (ZO-1, ZO-2, and ZO-3), which are ti ..., and * USP9X. References Further reading * * * * * * * * * * * * * * * * * * * {{PDB Gallery, geneid=4301 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Scaffold Protein
In biology, scaffold proteins are crucial regulators of many key signalling pathways. Although scaffolds are not strictly defined in function, they are known to interact and/or bind with multiple members of a signalling pathway, tethering them into complexes. In such pathways, they regulate signal transduction and help localize pathway components (organized in complexes) to specific areas of the cell such as the plasma membrane, the cytoplasm, the nucleus, the Golgi, endosomes, and the mitochondria. History The first signaling scaffold protein discovered was the Ste5 protein from the yeast ''Saccharomyces cerevisiae''. Three distinct domains of Ste5 were shown to associate with the protein kinases Ste11, Ste7, and Fus3 to form a multikinase complex. Function Scaffold proteins act in at least four ways: tethering signaling components, localizing these components to specific areas of the cell, regulating signal transduction by coordinating positive and negative feedback s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
