|
Bin-Amphiphysin-RVS
In molecular biology, BAR domains are highly conserved protein dimerisation domains that occur in many proteins involved in membrane dynamics in a cell. The BAR domain is banana-shaped and binds to membrane via its concave face. It is capable of sensing membrane curvature by binding preferentially to curved membranes. BAR domains are named after three proteins that they are found in: Bin, Amphiphysin and Rvs. BAR domains occur in combinations with other domains Many BAR family proteins contain alternative lipid specificity domains that help target these protein to particular membrane compartments. Some also have SH3 domains that bind to dynamin and thus proteins like amphiphysin and endophilin are implicated in the orchestration of vesicle scission. N-BAR domain Some BAR domain containing proteins have an N-terminal amphipathic helix preceding the BAR domain. This helix inserts (like in the epsin ENTH domain) into the membrane and induces curvature, which is stabilise ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
IMD Domain
In molecular biology, the IMD domain (IRSp53 and MIM (missing in metastases) homology Domain) is a BAR-like domain of approximately 250 amino acids found at the N-terminus in the insulin receptor tyrosine kinase substrate p53 (IRSp53/BAIAP2) and in the evolutionarily related IRSp53/MIM (MTSS1) family. In IRSp53, a ubiquitous regulator of the actin cytoskeleton, the IMD domain acts as conserved F-actin bundling domain involved in filopodium formation. Filopodium-inducing IMD activity is regulated by Cdc42 and Rac1 (Rho-family GTPases) and is SH3-independent. The IRSp53/MIM family is a novel F-actin bundling protein family that includes invertebrate relatives: * Vertebrate MIM (missing in metastasis) (MTSS1), an actin-binding scaffold protein that may be involved in cancer metastasis. * Vertebrate ABBA-1 ( MTSS1L), a MIM-related protein. *Vertebrate brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI1-associated protein 2) or insulin receptor tyrosine kinase subs ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amphiphysin
Amphiphysin is a protein that in humans is encoded by the ''AMPH'' gene. Function This gene encodes a protein associated with the cytoplasmic surface of synaptic vesicles. A subset of patients with stiff person syndrome who were also affected by breast cancer are positive for autoantibodies against this protein. Alternate splicing of this gene results in two transcript variants encoding different isoforms. Additional splice variants have been described, but their full length sequences have not been determined. Amphiphysin is a brain-enriched protein with an N-terminal lipid interaction, dimerisation and membrane bending BAR domain, a middle clathrin and adaptor binding domain and a C-terminal SH3 domain. In the brain, its primary function is thought to be the recruitment of dynamin to sites of clathrin-mediated endocytosis. There are 2 mammalian amphiphysins with similar overall structure. A ubiquitous splice form of amphiphysin-2 (BIN1) that does not contain clathrin or adapto ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sorting Nexin
Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain (a phospholipid-binding motif) or through protein–protein interactions with membrane-associated protein complexes Some members of this family have been shown to facilitate protein sorting. Family members In humans, sorting nexins are transcribed from the following genes: Structure Sorting nexins either consist solely of a PX domain (e.g. SNX3) or have a modular structure made up of the PX and additional domains. A subgroup of sorting nexins (comprising, in humans, SNX1, SNX2, SNX4, SNX5, SNX6, SNX7, SNX8, SNX9, SNX18, SNX30, SNX32 and SNX33) possess a BAR domain at their C-terminus. (The BAR domain of SNXs 1, 2, 4, 7, 8 and 30 is classified by pfam as 'Vps5 C terminal like'.) An example of a sorting nexin domain structure can be seen here for SNX1: # NTD – N-terminal domain # PX doma ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Development (journal)
''Development'' is a bi-weekly peer-reviewed scientific journal in the field of developmental biology that covers cellular and molecular mechanisms of animal and plant development. It is published by The Company of Biologists. ''Development'' is partnered with Publons, is part of the Review Commons initiative and has two-way integration with bioRxiv. In 2009, the BioMedical & Life Sciences Division of the Special Libraries Association included ''Development'' in their list of top 100 journals in Biology and Medicine over the last 100 years. Brief history Originally called ''Journal of Embryology and Experimental Morphology'' () and established in 1953, the journal provided a periodical that would be primarily devoted to morphogenesis. In 1987, the journal was renamed ''Development''. The journal's full archive from 1953 is available online. ''Development'' is now a hybrid journal and publishes 24 issues a year. Content over 6 months old is free to read. Scope and content ''De ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Traffic (journal)
''Traffic'' is a monthly, peer-reviewed, scientific journal, which was established in 2000, and is published by Wiley-Blackwell. The online version is at the Wiley Online Library. This journal is co-edited by Eric Chevet, Antonella De Matteis, Eeva-Liisa Eskelinen, and Hesso Farhan. The journal covers all aspects of signal transduction (intracellular transport) in health and disease, for both mammalian and non-mammalian biological systems. History The journal was established by Frances Brodsky, Mark Marsh, Sandra Schmid, and Thomas Kreis. Kreis died in a plane crash before the first issue was published. Abstracting and indexing This journal is abstracted and indexed in: According to the ''Journal Citation Reports'', the journal has a 2020 impact factor The impact factor (IF) or journal impact factor (JIF) of an academic journal is a scientometric index calculated by Clarivate that reflects the yearly mean number of citations of articles published in the last two years in a giv ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Membrane Curvature
Membrane curvature is the geometrical measure or characterization of the curvature of membranes. The membranes can be naturally occurring or man-made (synthetic). An example of naturally occurring membrane is the lipid bilayer of cells, also known as cellular membranes. Synthetic membranes can be obtained by preparing aqueous solutions of certain lipids. The lipids will then "aggregate" and form various phases and structures. According to the conditions (concentration, temperature, ionic strength of solution, etc.) and the chemical structures of the lipid, different phases will be observed. For instance, the lipid POPC (palmitoyl oleyl phosphatidyl choline) tends to form lamellar vesicles in solution, whereas smaller lipids (lipids with shorter acyl chains, up to 8 carbons in length), such as detergents, will form micelles if the CMC (critical micelle concentration) was reached. There are five commonly proposed mechanisms by which membrane curvature is created, maintained, or control ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Epsin
Epsins are a family of highly conserved membrane proteins that are important in creating membrane curvature. Epsins contribute to membrane deformations like endocytosis, and block Vesicle (biology), vesicle formation during mitosis. Structure Epsin contains various protein domains that aid in function. Starting at the N-terminus is the ENTH domain. ENTH stands for Epsin N-Terminal Homolog. The ENTH domain is approximately 150 amino acids long and is highly conserved across species. It is composed of seven Alpha helix, α-helices and an eighth helix that is not aligned with the seven helices that make up a superhelical fold. The role of the ENTH domain is to bind membrane lipids which is currently thought to aid in the invagination of the plasma membrane to form clathrin-coated vesicles. Additionally, located toward the C-terminus of the ENTH domain are two to three ubiquitin interacting motifs which aids in ubiquitin dependent recruitment. Following the ENTH domain there is not ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PX Domain
The PX domain is a phosphoinositide-binding structural domain involved in targeting of proteins to cell membranes. This domain was first found in P40phox and p47phox domains of NADPH oxidase (phox stands for phagocytic oxidase). It was also identified in many other proteins involved in membrane trafficking, including nexins, Phospholipase D, and phosphoinositide-3- kinases. The PX domain is structurally conserved in eukaryotes, although amino acid sequences show little similarity. PX domains interact primarily with PtdIns(3)P lipids. However some of them bind to phosphatidic acid, PtdIns(3,4)P2, PtdIns(3,5)P2, PtdIns(4,5)P2, and PtdIns(3,4,5)P3. The PX-domain can also interact with other domains and proteins. Human proteins containing this domain Sorting nexins contain this domain. Other examples include: * HS1BP3 * KIF16B (SNX23) * NCF1; NCF1C; NCF4; NISCH * PIK3C2A; PIK3C2B; PIK3C2G; PLD1; PLD2; PXK * RPS6KC1 * SGK3; SH3PXD2A; SNAG1; SNX9 Sorting nexin-9 is ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SNX8
The SNX8 is a sorting nexin protein involved in intracellular molecular traffic from the early endosomes to the TGN. It is suggested that it acts as an adaptor protein in events related to immune response and cholesterol regulation, for example. As a protein of the SNXs family, the SNX8 is formed of 465 aminoacids and presents a BAR-domain and a PX-domain which are very relevant in relation to its functions. Furthermore, SNX8 study is motivated by its medical significance in relation to diseases such as Alzheimer's Disease, cancer, neurodevelopmental malformations and to its role in fighting against viral infections. Structure Sorting nexins (SNXs) SNX8 belongs to the sorting nexin family of proteins, which mainly contain two functional membrane-binding that allow SNXs to have different roles in endosomal sorting and protein trafficking thanks to its membrane curvature ability. To begin with, SNX-PX is a distinct phosphoinositide (PI)-binding domain. The preferential interacti ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
