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Search results 1 to 12 out of 12 for Eps15

Category restricted to ProteinDomain (x)

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Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Domain
Description: Stonin 2 is involved in clathrin mediated endocytosis []. It binds to Eps15 by its highly conserved NPF motif. The complex formed has been shown to directly associate with the clathrin adaptor complex AP-2, and to localize to clathrin-coated pits (CCPs) []. In addition, stonin2 was recently identified as a specific sorting adaptor for synaptotagmin, and may thus regulate synaptic vesicle recycling []. This entry represents the N-terminal domain of stonin-2. It is found in association with .
Protein Domain
Type: Domain
Description: The EH (for Eps15 Homology) domain is a protein-protein interaction module of approximately 95 residues which was originally identified as a repeated sequence present in three copies at the N terminus of the tyrosine kinase substrates Eps15 and Eps15R [, ]. The EH domain was subsequently found in several proteins implicated in endocytosis, vesicle transport and signal transduction in organisms ranging from yeast to mammals. EH domains are present in one to three copies and they may include calcium-binding domains of the EF-hand type [, ]. Eps15 is divided into three domains: domain I contains signatures of a regulatory domain, including a candidate tyrosine phosphorylation site and EF-hand-type calcium-binding domains, domain II presents the characteristic heptad repeats of coiled-coil rod-like proteins, and domain III displays a repeated aspartic acid-proline-phenylalanine motif similar to a consensus sequence of several methylases [].EH domains have been shown to bind specifically but with moderate affinity to peptides containing short, unmodified motifs through predominantly hydrophobic interactions. The target motifs are divided into three classes: class I consists of the concensus Asn-Pro-Phe (NPF) sequence; class II consists of aromatic and hydrophobic di- and tripeptide motifs, including the Phe-Trp (FW), Trp-Trp (WW), and Ser-Trp-Gly (SWG) motifs; and class III contains the His-(Thr/Ser)-Phe motif (HTF/HSF) [, ]. The structure of several EH domains has been solved by NMR spectroscopy. The fold consists of two helix-loop-helix characteristic of EF-hand domains, connected by a short antiparallel β-sheet. The target peptide is bound in a hydrophobic pocket between two alpha helices. Sequence analysis and structural data indicate that not all the EF-hands are capable of binding calcium because of substitutions of the calcium-liganding residues in the loop [, , ]. This domain is often implicated in the regulation of protein transport/sorting and membrane trafficking. Messenger RNA translation initiation and cytoplasmic poly(A) tail shortening require the poly(A)-binding protein (PAB) in yeast. The PAB-dependent poly(A) ribonuclease (PAN) is organised into distinct domains containing repeated sequence elements [].
Protein Domain
Type: Domain
Description: SGIP1 is a member of the muniscin family. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis [], and is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15 [].The muniscins are a family of endocytic adaptors that is conserved from yeast to humans. Their C-terminal domain is structurally similar to mu homology domains (MHDs), and is the region of the muniscin proteins involved in the interactions with the endocytic adaptor-scaffold proteins Ede1-eps15 []. This entry represent the mu-homology domain (MHD) of SGIP1. Unlike other muniscins, SGIP1 does not contain the EFC/F-BAR domain, but does have a proline-rich domain (PRD) and a C-terminal MHD.
Protein Domain
Type: Domain
Description: This is the AAA ATPase domain found at the C-terminal of plant senescence-associated proteins and spartin. In Hemerocallis, petals have a genetically based program that leads to senescence and cell death approximately 24 hours, after the flower opens, and it is believed that senescence proteins produced around that time have a role in this program []. This domain is also found at the C-terminal of Spartin, a protein from higher vertebrates associated with endosomal trafficking and microtubule dynamics []. Spartin functions presynaptically with endocytic adaptor Eps15 to regulate synaptic growth and function. Mutations in human spartin gene cause Troyer syndrome, a hereditary spastic paraplegia []. This AAA ATPase domain similar to other AAA proteins contain an α/β nucleotide-binding domain (NBD) and a smaller four-helix bundle domain (HBD) []. Uniquely among AAA structures, spastin has two helices (N-terminal α1 and C-terminal α11) that embrace the NBD [].
Protein Domain
Type: Domain
Description: Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction []. It plays a role in clathrin-coated pit (CCP) formation []. It binds to many proteins through its multidomain structure and facilitates the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation []. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. This entry represents the first SH3 domain of ITSN2.
Protein Domain
Type: Domain
Description: Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction []. It plays a role in clathrin-coated pit(CCP) formation []. It binds to many proteins through its multidomain structure and facilitates the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation []. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. This entry represents the second SH3 domain of ITSN2.
Protein Domain
Type: Domain
Description: Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction []. It plays a role in clathrin-coated pit (CCP) formation []. It binds to many proteins through its multidomain structure and facilitates the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation []. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. This entry represents the third SH3 domain of ITSN2.
Protein Domain
Type: Domain
Description: Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction []. It plays a role in clathrin-coated pit (CCP) formation []. It binds to many proteins through its multidomain structure and facilitates the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation []. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. This entry represents the fourth SH3 domain of ITSN2.
Protein Domain
Type: Domain
Description: Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction []. It plays a role in clathrin-coated pit (CCP) formation []. It binds to many proteins through its multidomain structure and facilitates the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation []. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. This entry represents the fifth SH3 domain of ITSN2.
Protein Domain
Type: Domain
Description: The adaptor proteins AP-1 and GGA (Golgi-localized, gamma ear-containing, ADP-ribosylation factor (ARF)-binding proteins) regulate membrane traffic betweenthe trans-Golgi network (TGN) and endosome/lysosomes through ARF-regulatedmembrane association, recognition of sorting signals, and recruitment ofclathrin and accessory proteins. The gamma-adaptin ear (GAE) domain is a C-terminal appendage or ear of about 120 residues, which is found in gamma-adaptins, the heavy subunits of the AP-1 complex, and in GGAs. The GAE domain,which is found in associated with other domains such as VHS,coiled-coils and GAT, is involved in the recruitment of accessory proteins,such as gamma-synergin, Rababptin-5, Eps15 and cyclin G-associated kinase,which modulate the functions of GAE domain containing proteins in the membranetrafficking events [, , , ].The resolution of the 3D-structure of the human gamma-adaptin GAE domain shows that it forms an immunoglobulin-like β-sandwich fold composed of eightβ-strands with two short α-helices. The topology ofthe entire GAE domain is similar to those of the N-terminal subdomains in thealpha- and beta-adaptin ear domains of the AP-2 complex. However, the GAEdomain has very low sequence identity and homology to the N-terminalimmunoglobulin-like subdomains of the alpha and beta ear domains. The bindingsite for the accessory proteins has been located to a shallow hydrophobictrough surrounded by charged (mainly basic) residues [, ].This entry represents the entire GAE domain.
Protein Domain
Type: Domain
Description: This entry represents the dynamin-type guanine nucleotide-binding (G) domain. Members of the dynamin GTPase family appear to be ubiquitous. They catalyze diverse membrane remodelling events in endocytosis, cell division, and plastid maintenance. Their functional versatility also extends to other core cellular processes, such as maintenance of cell shape or centrosome cohesion. Members of the dynamin family are characterised by their common structure and by conserved sequences in the GTP-binding domain. The minimal distinguishing architectural features that are common to all dynamins and are distinct from other GTPases are the structure of the large GTPase domain (~280 amino acids) and the presence of two additional domains: the middle domain and the GTPase effector domain (GED), which are involved in oligomerization and regulation of the GTPase activity. In many dynamin family members, the basic set of domains is supplemented by targeting domains, such as: pleckstrin-homology (PH) domain, proline-rich domains (PRDs), or by sequences that target dynamins to specific organelles, such as mitochondria and chloroplasts [, , ]. The dynamin-type G domain consists of a central eight-stranded β-sheetsurrounded by seven alpha helices and two one-turn helices.It contains the five canonical guanine nucleotide binding motifs (G1-5). TheP-loop (G1) motif (GxxxxGKS/T) is also present in ATPases (Walker A motif) andfunctions as a coordinator of the phosphate groups of the bound nucleotide. Aconserved threonine in switch-I (G2) and the conserved residues DxxG ofswitch-II (G3) are involved in Mg(2+) binding and GTP hydrolysis. Thenucleotide binding affinity of dynamins is typically low, with specificity forGTP provided by the mostly conserved N/TKxD motif (G4). The G5 or G-cap motifis involved in binding the ribose moiety [, , ].Some proteins containing a dynamin-type G domain are listed below [, ]:Animal dynamin, the prototype for this family. The role of dynamin inendocytosis is well established. Additional roles were proposed in vesiclebudding from the trans-Golgi network (TGN) and the budding of caveolae fromthe plasma membrane [].Vetebrate Mx proteins, a group of interferon (IFN)-induced GTPases involvedin the control of intracellular pathogens [, ].Eukaryotic Drp1 (Dnm1 in yeast) mediates mitochondrial and peroxisomalfission.Eukaryotic Eps15 homology (EH)-domain-containing proteins (EHDs), ATPasesimplicated in clathrin-independent endocytosis and recycling fromendosomes. The dynamin-type G domains of EHDs bind to adenine rather thanto guanine nucleotide [, ].Yeast to human OPA1/Mgm1 proteins. They are found between the inner andouter mitochondrial membranes and are involved in mitochondrial fusion.Yeast to human mitofusin/fuzzy onions 1 (Fzo1) proteins, involved inmitochondrial dynamics [, ].Yeast vacuolar protein sorting-associated protein 1 (Vps1), involved invesicle trafficking from the Golgi.Escherichia coli clamp-binding protein CrfC (or Yjda), important for thecolocalization of sister nascent DNA strands after replication fork passageduring DNA replication, and for positioning and subsequent partitioning ofsister chromosomes [].Nostoc punctiforme bacterial dynamin-like protein (BDLP) [, ].
Protein Domain
Type: Homologous_superfamily
Description: Proteins synthesized on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. These vesicles have specific coat proteins (such as clathrin or coatomer) that are important for cargo selection and direction of transport []. Clathrin coats contain both clathrin (acts as a scaffold) and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The two major types of clathrin adaptor complexes are the heterotetrameric adaptor protein (AP) complexes, and the monomeric GGA (Golgi-localising, Gamma-adaptin ear domain homology, ARF-binding proteins) adaptors [, ].AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and lipids to clathrin at vesicle budding sites, as well as binding accessory proteins that regulate coat assembly and disassembly (such as AP180, epsins and auxilin). There are different AP complexes in mammals. AP1 is responsible for the transport of lysosomal hydrolases between the TGN and endosomes []. AP2 associates with the plasma membrane and is responsible for endocytosis []. AP3 is responsible for protein trafficking to lysosomes and other related organelles []. AP4 is less well characterised. AP complexes are heterotetramers composed of two large subunits (adaptins), a medium subunit (mu) and a small subunit (sigma). For example, in AP1 these subunits are gamma-1-adaptin, beta-1-adaptin, mu-1 and sigma-1, while in AP2 they are alpha-adaptin, beta-2-adaptin, mu-2 and sigma-2. Each subunit has a specific function. Adaptins recognise and bind to clathrin through their hinge region (clathrin box), and recruit accessory proteins that modulate AP function through their C-terminal ear (appendage) domains. Mu recognises tyrosine-based sorting signals within the cytoplasmic domains of transmembrane cargo proteins []. One function of clathrin and AP2 complex-mediated endocytosis is to regulate the number of GABA(A) receptors available at the cell surface []. This entry represents a β-sandwich structural motif found in the appendage (ear) domain of gamma1-adaptin from AP1 clathrin adaptor complex, and the homologous C-terminal GAE (gamma-adaptin ear) domain of GGA adaptor proteins. These domains have an immunoglobulin-like β-sandwich fold containing 8 strands in 2 β-sheets in a Greek key topology [, ]. This is a similar fold to that found in alpha- and beta-adaptins, but there is little sequence identity between them. The GAE domain is involved in the recruitment of accessory proteins, such as gamma-synergin, Rababptin-5, Eps15 and cyclin G-associated kinase, which modulate the functions of GAE domain containing proteins in the membrane trafficking events [, ]. The binding site in GAE for accessory proteins is located in a shallow hydrophobic trough surrounded by charged (mainly basic) residues [].