Vann Bennett

Journal article Nature · February 6, 2003 Featured Publication Mutations in ion channels involved in the generation and termination of action potentials constitute a family of molecular defects that underlie fatal cardiac arrhythmias in inherited long-QT syndrome. We report here that a loss-of-function (E1425G) mutati ... Full text Link to item Cite

A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin.

Journal article J Neurosci · September 15, 2002 Featured Publication Doublecortin is a cytoplasmic protein mutated in the neuronal migration disorder X-linked lissencephaly. This study describes a novel activity of doublecortin in recognition of the FIGQY-phosphotyrosine motif present in the cytoplasmic domain of the L1 cel ... Full text Link to item Cite

Ankyrins.

Journal article J Cell Sci · April 15, 2002 Featured Publication Full text Link to item Cite

The ankyrin-B C-terminal domain determines activity of ankyrin-B/G chimeras in rescue of abnormal inositol 1,4,5-trisphosphate and ryanodine receptor distribution in ankyrin-B (-/-) neonatal cardiomyocytes.

Journal article J Biol Chem · March 22, 2002 Featured Publication Ankyrins are a closely related family of membrane adaptor proteins that are believed to participate in targeting diverse membrane proteins to specialized domains in the plasma membrane and endoplasmic reticulum. This study addresses the question of how ind ... Full text Link to item Cite

Developing nodes of Ranvier are defined by ankyrin-G clustering and are independent of paranodal axoglial adhesion.

Journal article Proc Natl Acad Sci U S A · February 19, 2002 Featured Publication Nodes of Ranvier are excitable regions of axonal membranes highly enriched in voltage-gated sodium channels that propagate action potentials. The mechanism of protein clustering at nodes has been a source of controversy. In this study, developmental analys ... Full text Link to item Cite

Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments.

Journal article J Cell Biol · November 26, 2001 Featured Publication The axon initial segment is an excitable membrane highly enriched in voltage-gated sodium channels that integrates neuronal inputs and initiates action potentials. This study identifies Nav1.6 as the voltage-gated sodium channel isoform at mature Purkinje ... Full text Link to item Cite

FIGQY phosphorylation defines discrete populations of L1 cell adhesion molecules at sites of cell-cell contact and in migrating neurons.

Journal article J Cell Sci · November 2001 Featured Publication Phosphorylation of neurofascin, a member of the L1 family of cell adhesion molecules (L1 CAMs), at the conserved FIGQY-tyrosine abolishes the ankyrin-neurofascin interaction. This study provides the first evidence, in Drosophila melanogaster and vertebrate ... Full text Link to item Cite

LAD-1, the Caenorhabditis elegans L1CAM homologue, participates in embryonic and gonadal morphogenesis and is a substrate for fibroblast growth factor receptor pathway-dependent phosphotyrosine-based signaling.

Journal article J Cell Biol · August 20, 2001 Featured Publication This study shows that L1-like adhesion (LAD-1), the sole Caenorhabditis elegans homologue of the L1 family of neuronal adhesion molecules, is required for proper development of the germline and the early embryo and embryonic and gonadal morphogenesis. In a ... Full text Link to item Cite

Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues.

Journal article Physiol Rev · July 2001 Featured Publication The spectrin-based membrane skeleton of the humble mammalian erythrocyte has provided biologists with a set of interacting proteins with diverse roles in organization and survival of cells in metazoan organisms. This review deals with the molecular physiol ... Full text Link to item Cite

Ankyrins and cellular targeting of diverse membrane proteins to physiological sites.

Journal article Curr Opin Cell Biol · February 2001 Featured Publication Ankyrins are spectrin-binding proteins that associate via ANK repeats with a variety of ion channels/pumps, calcium release channels and cell adhesion molecules. Recent studies in mice indicate that ankyrins have a physiological role in restricting voltage ... Full text Link to item Cite

Caenorhabditis elegans beta-G spectrin is dispensable for establishment of epithelial polarity, but essential for muscular and neuronal function.

Journal article J Cell Biol · May 15, 2000 Featured Publication The Caenorhabditis elegans genome encodes one alpha spectrin subunit, a beta spectrin subunit (beta-G), and a beta-H spectrin subunit. Our experiments show that the phenotype resulting from the loss of the C. elegans alpha spectrin is reproduced by tandem ... Full text Link to item Cite

Abnormal cardiac Na(+) channel properties and QT heart rate adaptation in neonatal ankyrin(B) knockout mice.

Journal article Circ Res · March 3, 2000 Featured Publication The cytoskeleton of the cardiomyocyte has been shown to modulate ion channel function. Cytoskeletal disruption in vitro alters Na(+) channel kinetics, producing a late Na(+) current that can prolong repolarization. This study describes the properties of th ... Full text Link to item Cite

Ankyrin-B is required for intracellular sorting of structurally diverse Ca2+ homeostasis proteins.

Journal article J Cell Biol · November 29, 1999 Featured Publication This report describes a congenital myopathy and major loss of thymic lymphocytes in ankyrin-B (-/-) mice as well as dramatic alterations in intracellular localization of key components of the Ca(2+) homeostasis machinery in ankyrin-B (-/-) striated muscle ... Full text Link to item Cite

Nervous system defects of AnkyrinB (-/-) mice suggest functional overlap between the cell adhesion molecule L1 and 440-kD AnkyrinB in premyelinated axons.

Journal article J Cell Biol · November 30, 1998 Featured Publication The L1 CAM family of cell adhesion molecules and the ankyrin family of spectrin-binding proteins are candidates to collaborate in transcellular complexes used in diverse contexts in nervous systems of vertebrates and invertebrates. This report presents evi ... Full text Link to item Cite

AnkyrinG is required for clustering of voltage-gated Na channels at axon initial segments and for normal action potential firing.

Journal article J Cell Biol · November 30, 1998 Featured Publication Voltage-gated sodium channels (NaCh) are colocalized with isoforms of the membrane-skeletal protein ankyrinG at axon initial segments, nodes of Ranvier, and postsynaptic folds of the mammalian neuromuscular junction. The role of ankyrinG in directing NaCh ... Full text Link to item Cite

Adducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons.

Journal article J Cell Biol · July 27, 1998 Featured Publication Adducin is a heteromeric protein with subunits containing a COOH-terminal myristoylated alanine-rich C kinase substrate (MARCKS)-related domain that caps and preferentially recruits spectrin to the fast-growing ends of actin filaments. The basic MARCKS-rel ... Full text Link to item Cite

Tyrosine phosphorylation at a site highly conserved in the L1 family of cell adhesion molecules abolishes ankyrin binding and increases lateral mobility of neurofascin.

Journal article J Cell Biol · May 5, 1997 Featured Publication This paper presents evidence that a member of the L1 family of ankyrin-binding cell adhesion molecules is a substrate for protein tyrosine kinase(s) and phosphatase(s), identifies the highly conserved FIGQY tyrosine in the cytoplasmic domain as the princip ... Full text Link to item Cite

AnkyrinG. A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier.

Journal article J Biol Chem · February 3, 1995 Featured Publication We have characterized a new ankyrin gene, expressed in brain and other tissues, that is subject to extensive tissue-specific alternative mRNA processing. The full-length polypeptide has a molecular mass of 480 kDa and includes a predicted globular head dom ... Full text Link to item Cite

Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively spliced genes.

Journal article J Cell Biol · July 1991 Featured Publication Ankyrins are a family of membrane-associated proteins that can be divided into two immunologically distinct groups: (a) erythrocyte-related isoforms (ankyrinR) that have polarized distributions in particular cell types; and (b) brain-related isoforms (anky ... Full text Link to item Cite

Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins.

Journal article Nature · March 1, 1990 Featured Publication Analysis of complementary DNA for human erythroid ankyrin indicates that the mature protein contains 1,880 amino acids comprising an N-terminal domain binding integral membrane proteins and tubulin, a central domain binding spectrin and vimentin, and an ac ... Full text Link to item Cite

Brain spectrin, a membrane-associated protein related in structure and function to erythrocyte spectrin.

Journal article Nature · September 9, 1982 Featured Publication An immunoreactive analogue of erythrocyte spectrin has been purified from brain membranes. This protein co-sediments with and cross-links actin filaments, associates with spectrin-binding sites on erythrocyte membranes, and has been visualized by rotary sh ... Full text Link to item Cite

Immunoreactive forms of human erythrocyte ankyrin are present in diverse cells and tissues.

Journal article Nature · October 18, 1979 Featured Publication Ankyrin is a polypeptide of molecular weight (MW) 200,000 which is tightly bound to the cytoplasmic surface of the human erythrocyte membrane and has been identified as the high-affinity membrane attachment protein for spectrin. This protein has also been ... Full text Link to item Cite

The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes.

Journal article Nature · August 9, 1979 Featured Publication Ankyrin, the membrane attachment protein for human erythrocyte spectrin, is tightly linked in a 1:1 molar ratio with band 3 in detergent extracts of spectrin-depleted membranes. Ankyrin-linked band 3, which represents 10--15% of the total band 3, spans the ... Full text Link to item Cite

Purification of an active proteolytic fragment of the membrane attachment site for human erythrocyte spectrin.

Journal article J Biol Chem · April 10, 1978 Featured Publication Link to item Cite