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Spectrin, beta, non-erythrocytic 4

betaIV spectrin, beta4-spectrin
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 organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. This gene is one member of a family of beta-spectrin genes. The encoded protein localizes to the nuclear matrix, PML nuclear bodies, and cytoplasmic vesicles. A highly similar gene in the mouse is required for localization of specific membrane proteins in polarized regions of neurons. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
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Top mentioned proteins: ankyrin-G, NODAL, Neurofascin, Bravo, CAN
Papers on betaIV spectrin
A new paraneoplastic encephalomyelitis autoantibody reactive with the axon initial segment.
Smitt et al., Netherlands. In Neurosci Lett, 2010
Double labeling experiments and absence of staining at the nodes of Ranvier excluded the previously identified betaIV spectrin as autoantigen.
Disruption of the axon initial segment cytoskeleton is a new mechanism for neuronal injury.
Rasband et al., Farmington, United States. In J Neurosci, 2009
Furthermore, we show this is caused by proteolysis of the AIS cytoskeletal proteins ankyrinG and betaIV spectrin by the calcium-dependent cysteine protease calpain.
Selective alterations in postsynaptic markers of chandelier cell inputs to cortical pyramidal neurons in subjects with schizophrenia.
Lewis et al., Pittsburgh, United States. In Neuropsychopharmacology, 2009
To understand the nature and functional significance of these alterations, we determined the density, laminar distribution, and length of AIS immunoreactive (IR) for ankryin-G and betaIV spectrin, two proteins involved in the regulation of synapse structure and ion channel clustering at AIS, in dlPFC area 46 from 14 matched triads of subjects with schizophrenia or major depressive disorder (MDD) and normal comparison participants.
Postnatal development of synaptic structure proteins in pyramidal neuron axon initial segments in monkey prefrontal cortex.
Lewis et al., Pittsburgh, United States. In J Comp Neurol, 2009
In order to understand the potential molecular mechanisms associated with these developmental refinements, we quantified the relative densities, laminar distributions, and lengths of pyramidal neuron AIS immunoreactive for ankyrin-G, betaIV spectrin, or gephyrin, three proteins involved in regulating synapse structure and receptor localization, in the PFC of rhesus monkeys ranging in age from birth through adulthood.
Neurofascin assembles a specialized extracellular matrix at the axon initial segment.
Rasband et al., Farmington, United States. In J Cell Biol, 2007
In addition to ion channels, these domains are characterized by cell adhesion molecules (CAMs; neurofascin-186 [NF-186] and neuron glia-related CAM [NrCAM]), cytoskeletal proteins (ankyrinG and betaIV spectrin), and the extracellular chondroitin-sulfate proteoglycan brevican.
Activity-regulated cytoskeleton-associated protein Arc/Arg3.1 binds to spectrin and associates with nuclear promyelocytic leukemia (PML) bodies.
VanDongen et al., Durham, United States. In Brain Res, 2007
Arc co-localized and interacted with the betaIV spectrin splice variant betaSpIVSigma5, a nuclear spectrin isoform associated with PML bodies and the nuclear matrix.
Nodes of Ranvier and axon initial segments are ankyrin G-dependent domains that assemble by distinct mechanisms.
Salzer et al., New York City, United States. In J Cell Biol, 2007
Both domains are enriched in sodium channels complexed with adhesion molecules (neurofascin [NF] 186 and NrCAM) and cytoskeletal proteins (ankyrin G and betaIV spectrin).
betaIV spectrin is recruited to axon initial segments and nodes of Ranvier by ankyrinG.
Rasband et al., Farmington, United States. In J Cell Biol, 2007
The organization of these membrane domains depends on a specialized cytoskeleton consisting of two submembranous cytoskeletal and scaffolding proteins, ankyrinG (ankG) and betaIV spectrin.
Expression of protein 4.1G in Schwann cells of the peripheral nervous system.
Ohno et al., Japan. In J Neurosci Res, 2006
Immunohistochemical staining with a 4.1G-specific antibody and double immunolabeling with E-cadherin, betaIV spectrin, and connexin 32 detected 4.1G in paranodal loops, Schmidt-Lanterman incisures, and periaxonal, mesaxonal, and abaxonal membranes of rodent sciatic nerve.
Spectrins and ankyrinB constitute a specialized paranodal cytoskeleton.
Rasband et al., Farmington, United States. In J Neurosci, 2006
In contrast, genetic disruption of the juxtaparanodal protein Caspr2 or the nodal cytoskeletal protein betaIV spectrin did not alter the paranodal cytoskeleton.
Neurofascin interactions play a critical role in clustering sodium channels, ankyrin G and beta IV spectrin at peripheral nodes of Ranvier.
Grumet et al., United States. In Dev Biol, 2006
NF-Fc significantly inhibited nodal clustering of Na+ channels, ankyrin G, and betaIV spectrin, and modestly reduced Caspr clustering at paranodal junctions; it did not significantly affect lengths or numbers of myelin-positive segments, axon initial segments, or accumulations of phosphorylated-ERM proteins in Schwann cell nodal microvilli.
BetaIVSigma1 spectrin stabilizes the nodes of Ranvier and axon initial segments.
Solimena et al., Dresden, Germany. In J Cell Biol, 2004
Here, we prove that betaIVSigma1 spectrin, the only betaIV spectrin with an actin-binding domain, is an essential component of this coat.
BetaIV spectrins are essential for membrane stability and the molecular organization of nodes of Ranvier.
Rasband et al., Farmington, United States. In J Neurosci, 2004
To investigate the molecular organization of nodes, we analyzed qv(3J)"quivering" mice, whose betaIV spectrins have a truncated proline-rich "specific" domain (SD) and lack the pleckstrin homology (PH) domain.
Protein disulfide bond formation in the cytoplasm during oxidative stress.
Schubert et al., Los Angeles, United States. In J Biol Chem, 2004
In addition, an epitope-tagged version of the molecular chaperone HSP70 forms mixed disulfides with both beta4-spectrin and adenomatous polyposis coli protein in the cytosol.
DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation.
Austin et al., United States. In Hum Mol Genet, 2003
DISC1 interacts by yeast two-hybrid, mammalian two-hybrid, and co-immunoprecipitation assays with multiple proteins of the centrosome and cytoskeletal system, including MIPT3, MAP1A and NUDEL; proteins which localize receptors to membranes, including alpha-actinin2 and beta4-spectrin; and proteins which transduce signals from membrane receptors, including ATF4 and ATF5.
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