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Search results 1 to 5 out of 5 for Pick1

Category restricted to ProteinDomain (x)

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Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Domain
Description: Protein Interacting with C Kinase 1 (PICK1) is highly expressed in brain and testes. It plays a key role in the trafficking of AMPA receptors, which are critical for regulating synaptic strength and may be important in cellular processes involved in learning and memory [, ]. PICK1 is also critical in the early stages of spermiogenesis. Mice deficient in PICK1 are infertile and show characteristics of the human disease globozoospermia such as round-headed sperm, reduced sperm count, and severely impaired sperm motility []. PICK1 may also be involved in the neuropathogenesis of schizophrenia [].PICK1 contains an N-terminal PDZ domain and a C-terminal BAR domain [], also designated as AH (arfaptin homology) domain []. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of PICK1 is necessary for its membrane localization and activation [, ].
Protein Domain
Type: Domain
Description: The arfaptin homology (AH) domain is a protein domain found in a range of proteins, including arfaptins, protein kinase C-binding protein PICK1 []and mammalian 69kDa islet cell autoantigen (ICA69) []. The AH domain of arfaptin has been shown to dimerise and to bind Arf and Rho family GTPases [, ], including ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules.The AH domain consists of three α-helices arranged as an extended antiparallel α-helical bundle. Two arfaptin AH domains associate to form a highly elongated, crescent-shaped dimer [, ].
Protein Domain
Type: Family
Description: This family consists of Arfaptin-1, Arfaptin-2, and protein kinase C-binding protein 1 (PICK1). They all contain a Bin/amphiphysin/Rvs (BAR) domain []. BAR-domain-containing proteins are key players in membrane dynamics as their crescent shape allows them to sense or generate curvature on lipid bilayers [].Arfaptin-1 and 2 have been shown to interact with Arf GTPases and Arf-like 1 (Arl1). They are recruited to trans-Golgi membranes through interaction with Arl1 [].In neurons, PICK1 forms homodimers and serves as one of the scaffolding proteins that interacts with AMPA receptors and regulates their trafficking in synaptic plasticity []. In pancreatic beta cells, it forms heteromeric BAR-domain complexes with another cytosolic lipid-binding protein, ICA69. Together they are key regulators of the formation and maturation of insulin granules [].
Protein Domain
Type: Family
Description: Kelch-like protein 24 (KLHL24, also known as KRIP6) belongs to the KLHL family []. KRIP6 binds to and regulates the GluR6a kainate receptor []. It also modulates the interaction of PICK1 with GluR6 kainate receptors []. Kainate receptors (KAR) are ionotropic receptors that respond to the neurotransmitter glutamate and have been implicated in epilepsy, stroke, Alzheimer's and neuropathic pain [].The KLHL (Kelch-like) proteins generally have a BTB/POZ domain, a BACK domain, and five to six Kelch motifs. They constitute a subgroup at the intersection between the BTB/POZ domain and Kelch domain superfamilies. The BTB/POZ domain facilitates protein binding [], while the Kelch domain (repeats) form β-propellers. The Kelch superfamily of proteins can be subdivided into five groups: (1) N-propeller, C-dimer proteins, (2) N-propeller proteins, (3) propeller proteins, (4) N-dimer, C-propeller proteins, and (5) C-propeller proteins. KLHL family members belong to the N-dimer, C-propeller subclass of Kelch repeat proteins []. In addition to BTB/POZ and Kelch domains, the KLHL family members contain a BACK domain, first described as a 130-residue region of conservation observed amongst BTB-Kelch proteins []. Many of the Kelch-like proteins have been identified as adaptors for the recruitment of substrates to Cul3-based E3 ubiquitin ligases [, ].
Protein Domain
Type: Homologous_superfamily
Description: This superfamily represents a structural domain which consists of three α-helices, including the arfaptin homology (AH) domain and the BAR (Bin-Amphiphysin-Rvs) domain.The arfaptin homology (AH) domain is a protein domain found in a range of proteins, including arfaptins, protein kinase C-binding protein PICK1 []and mammalian 69kDa islet cell autoantigen (ICA69) []. The AH domain of arfaptin has been shown to dimerise and to bind Arf and Rho family GTPases [, ], including ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. The AH domain consists of three α-helices arranged as an extended antiparallel α-helical bundle. Two arfaptin AH domains associate to form a highly elongated, crescent-shaped dimer [, ].Members of the Amphiphysin protein family are key regulators in the early steps of endocytosis, involved in the formation of clathrin-coated vesicles by promoting the assembly of a protein complex at the plasma membrane and directly assist in the induction of the high curvature of the membrane at the neck of the vesicle. Amphiphysins contain a characteristic domain, known as the BAR (Bin-Amphiphysin-Rvs) domain, which is required for their in vivofunction and their ability to tubulate membranes []. The crystal structure of these proteins suggest the domain forms a crescent-shaped dimer of a three-helix coiled coil with a characteristic set of conserved hydrophobic, aromatic and hydrophilic amino acids. Proteins containing this domain have been shown to homodimerise, heterodimerise or, in a few cases, interact with small GTPases.