2 edition of Actin-binding proteins 1: spectrin superfamily found in the catalog.
Actin-binding proteins 1: spectrin superfamily
John H. Hartwig
|Statement||John H. Hartwig.|
|Series||Protein profile -- vol.2, issue 7|
Immunochemical detection of actin as well as spectrin-like proteins have been carried out in the green algae Micrasterias denticulata, Closterium lunula, and Euastrum these algae, actin is detected on Western blots at 43 kDa with antibodies to actin from higher plant and animal by: several families of actin-crosslinking proteins, and sequence analysis has revealed a homologous actin-binding domain in a large subset, referred to as the fimbrin, c~-actinin, filamin family , or as an actin crosslinker superfamily (, also see ). This domain is found in members of the spectrin superfamily .
Alpha-actinin is a cytoskeletal actin-binding protein and a member of the spectrin superfamily, which comprises spectrin, dystrophin and their homologues and isoforms. It forms an anti-parallel rod-shaped dimer with one actin-binding domain at each end of the rod and bundles actin filaments in multiple cell-type and cytoskeleton frameworks. In non-muscle cells, alpha-actinin is found Cited by: actin binding domains of dystrophin, plectin, fimbrin, and -ac-tinin are considered, these results suggest that the spectrin superfamily of proteins creates diverse structures with actin filaments because of the ability of the CH modules to rearrange on multiple binding sites within the actin subunit (18–21).
Spectrin is related to a large superfamily of actin cross-linking proteins that all share the CH domain actin binding motif. A closer-knit spectrin family of proteins shares the same general domain structure and molecular shape as human erythrocyte spectrin. features characteristic of the spectrin superfamily (Fig. 1) (Gregory and Brown, ; Strumpf and Volk, ; Leung et al., b). Proteins in this superfamily can be deﬁned by two features: (1) an N-terminal actin-binding domain; and (2) a section of α-helical spectrin repeats. The completion of the by:
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Get this from a library. Actin-binding proteins 1: spectrin superfamily. [John H Hartwig;]. Identification and functional characterization of protein R and actin-binding sites in erythrocyte beta spectrin: regulation of the interactions by phosphatidylinositol-4,5-bisphosphate. An X, Debnath G, Guo X, Liu S, Lux SE, Baines A, Gratzer W, Mohandas N.
Biochemistry, 44(31), 01 Aug Cited by: Proteins in the spectrin superfamily are composed of a series of triple helical repeats that serve as binding sites for other cytoskeletal proteins.
Spectrin also harbors a central SH3 domain and binding sites for Ca 2+ - activated proteins, suggesting that it may play a role in signaling cascades. The actin-binding domain (ABD) is limited to the N-terminal region of βI-spectrin and is composed of two Cited by: The actin-binding domain (ABD) of the spectrin family of proteins consists of two calponin-homology (CH1 and CH2) domains in tandem.
These ABDs are found near the amino termini of these proteins. Calponin, which is a calcium-binding protein present in smooth muscle, has a single CH domain that is not able to bind to by: speciﬁc Networked (NET) superfamily of actin-binding proteins, members of which localize to the actin cytoskel-eton and specify different membrane compartments.
The founding member of the NET superfamily, NET1A, is an-chored at the plasma membrane and predominates at cell junctions,1Abindsdirectlytoactin.
NET1A binds directly to actin filaments via a novel actin-binding domain that defines a superfamily of thirteen Arabidopsis proteins divided into four distinct phylogenetic by: The evolution of the actin binding NET superfamily. superfamily are plant-speciﬁc actin binding proteins of adaptor proteins, including α-actinin, spectrin, ﬁlamin, and Cited by: Structure of the Spectrin-Actin Binding Site of Erythrocyte Protein * (Received for publication, May 8, ) Isabel Correas, David W.
Speicher, and Vincent T. MarchesiS From the Yale University School of Medicine, Department of Pathology, New Haven, Connecticut The complete primary structure of the functional site of erythrocyte.
Spinocerebellar ataxia type 5 (SCA5) is a neurodegenerative disease caused by mutations in the cytoskeletal protein β-III-spectrin. Previously, a SCA5 mutation resulting in a Cited by: 8.
Spectrin is a large, cytoskeletal, and heterodimeric protein composed of modular structure of α and β subunits, it typically contains contiguous amino acid sequence motifs called “spectrin repeats”.
Spectrin is crucial for maintaining the stability and structure of the cell membrane and the shape of a cell. Moreover, it contributes to diverse cell functions such as cell adhesion Cited by: Spectrin alpha chain, erythrocyte is a protein that in humans is encoded by the SPTA1 gene. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of s: SPTA1, EL2, HPP, HS3, SPH3, SPTA, Spectrin.
Function. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and actinin is an actin-binding protein with multiple roles in different cell nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved Aliases: ACTN1, BDPLT15, actinin alpha 1.
The Networked (NET) proteins are a superfamily of plant-specific actin-binding proteins which localize simultaneously to the actin cytoskeleton and specific membrane compartments and are suggested to couple these membranes to the actin cytoskeleton in plant cells (Deeks et al., ).
Metazoans utilize a variety of adaptor proteins, including α-actinin, spectrin, filamin, and FERM-domain proteins Cited by: Interaptin, an Actin-binding Protein of the a nin superfamily, a Dictyostelium discoideum spectrin-like protein (Bennett and Condeelis, ).
Addi. Much new information on the sequence, structure, and function of filament crosslinking, capping, and severing proteins is now known. Other significant findings include identification of a new abundant monomer-sequestering protein in platelets, and evidence that many actin-binding proteins interact with phosphoinositides and that this interaction may have metabolic by: Utrophin is a large multidomain protein that belongs to a superfamily of actin-binding proteins, which includes dystrophin, alpha-actinin, beta-spectrin, fimbrin, filamin and plectin.
apparatus (for review see [1, 2]). Actin filaments are conserved family of actin-binding proteins – the most of the spectrin superfamily proteins, but also in.
proteins are often considered as spectrin and actin binding proteins, because of the importance of this activity to erythrocyte membrane properties. However, it is important to note that the fruitfly protein coracle does not have a spectrin–actin binding domain , and this applies to other simple invertebrates .Cited by: Actin-binding protein (also known as ABP) are proteins that bind to actin.
This may mean ability to bind actin monomers, or polymers, or both. Many actin-binding proteins, including α-actinin, β-spectrin, dystrophin, utrophin and fimbrin, do this through the actin-binding calponin homology domain. Calponin homology domain (or CH domain) is a family of actin binding domains found in both cytoskeletal proteins and signal transduction proteins.
The domain is about amino acids in length and is composed of four alpha helices. It comprises the following groups of actin-binding domains: Actinin-type (including spectrin, fimbrin, ABP)InterPro: IPR.
The three-dimensional structure of the calponin homology domain present in many actin binding cytoskeletal and signal-transducing proteins has been determined at A resolution. Actin-Binding Proteins 1: Spectrin Superfamily Hartwig, J.H. () Protein Profile 1: Cited by: Defining of the Minimal Domain of Protein Involved in Spectrin-Actin Binding.
Journal of Biological Chemistry(36), DOI: /jbc Michael B. Morris, Samuel E. Lux. Characterization of the Binary Interaction Between Human Erythrocyte Protein and by: Hauser et al. employ three-dimensional STORM super-resolution microscopy to resolve the actin-spectrin-based membrane cytoskeleton in neural stem cells (NSCs) and NSC-derived neurons, astrocytes, and oligodendrocytes, revealing a highly conserved one-dimensional periodic cytoskeletal motif that serves as a nanoscale scaffold and ruler for intercellular by: