Genomes and Genes
Gene Symbol: Epb4.1
Description: erythrocyte protein band 4.1
Alias: 4.1R, AI415518, D4Ertd442e, Elp-1, Elp1, Epb41, mKIAA4056, P4.1, Protein 4.1R, band 4.1, protein 4.1
- Impaired intestinal calcium absorption in protein 4.1R-deficient mice due to altered expression of plasma membrane calcium ATPase 1b (PMCA1b)Congrong Liu
Red Cell Physiology Laboratory, New York Blood Center, New York, New York 10065, USA
J Biol Chem 288:11407-15. 2013..1R and the second intracellular loop and C terminus of PMCA1b. Our findings have enabled us to define a functional role for 4.1R in small intestinal calcium absorption through regulation of membrane expression of PMCA1b...
- Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome-nucleus association and transcriptional signalingAdam J Meyer
Department of Genome Dynamics, University of California, Berkeley, CA 94720, USA
J Cell Sci 124:1433-44. 2011....
- Protein 4.1R regulates cell adhesion, spreading, migration and motility of mouse keratinocytes by modulating surface expression of beta1 integrinLixiang Chen
Red Cell Physiology Laboratory, New York Blood Center, New York, NY 10065, USA
J Cell Sci 124:2478-87. 2011..These data enabled the identification of a functional role for protein 4.1R in keratinocytes by modulating the surface expression of β1 integrin, possibly through a direct association between 4.1R and β1 integrin...
- Isoforms of protein 4.1 are differentially distributed in heart muscle cells: relation of 4.1R and 4.1G to components of the Ca2+ homeostasis systemJennifer C Pinder
King s College London, Randall Division of Cell and Molecular Biophysics, New Hunt s House, Guy s Campus, London SE1 1UL, UK
Exp Cell Res 318:1467-79. 2012..We conclude that isoforms of 4.1 proteins are differentially compartmentalised in the heart, and that they form specific complexes with proteins central to cardiomyocyte Ca(2+) metabolism...
- The 4.1B cytoskeletal protein regulates the domain organization and sheath thickness of myelinated axonsSteven Einheber
School of Health Sciences, Hunter College, City University of New York, New York, New York, USA
Glia 61:240-53. 2013..1B. These results demonstrate that 4.1B is a key cytoskeletal scaffold for axonal adhesion molecules expressed in the juxtaparanodal and internodal domains that unexpectedly regulates myelin sheath thickness...
- Quantitative analysis of murine terminal erythroid differentiation in vivo: novel method to study normal and disordered erythropoiesisJing Liu
Red Cell Physiology Laboratory, New York Blood Center, New York, NY, USA
Blood 121:e43-9. 2013..The means to quantitate in vivo murine erythropoiesis using our approach will probably have broad application in the study of altered erythropoiesis in various red cell disorders...
- The carboxyterminal EF domain of erythroid alpha-spectrin is necessary for optimal spectrin-actin bindingCatherine Korsgren
Division of Hematology Oncology, Department of Medicine, Children s Hospital Boston, Boston, MA 02115, USA
Blood 116:2600-7. 2010..1R complex. A model, based on the structure of α-actinin, suggests that the EF domain modulates the function of the ABD and that the C-terminal EF hands (EF(34)) may bind to the linker that connects the ABD to the first spectrin repeat...
- Protein 4.1 and the control of ion channelsAnthony J Baines
Department of Biosciences, University of Kent, Canterbury, CT2 7NJ Kent, UK
Blood Cells Mol Dis 42:211-5. 2009..A hypothesis to investigate in the future is that differential regulation of 4.1 and ankyrins (e.g. by PIP(2)) allows highly selective control of cell surface accumulation and transport activity of a specific range of ion channels...
- Cytoskeletal protein 4.1R negatively regulates T-cell activation by inhibiting the phosphorylation of LATQiaozhen Kang
Red Cell Physiology Laboratory, New York Blood Center, New York, NY 10065, USA
Blood 113:6128-37. 2009..1R display an elevated humoral response to immunization with T cell-dependent antigen. Thus, we have defined a hitherto unrecognized role for 4.1R in negatively regulating T-cell activation by modulating intracellular signal transduction...
- alphaII-betaV spectrin bridges the plasma membrane and cortical lattice in the lateral wall of the auditory outer hair cellsKirian Legendre
Institut Pasteur, Unite de Genetique et Physiologie de l Audition, 25 rue du Dr Roux, 75015 Paris, France
J Cell Sci 121:3347-56. 2008..We conclude that the cortical network involved in the sound-induced electromotility of OHCs contains alphaII-betaV spectrin, and not the conventional alphaII-betaII spectrin...
- Cytoskeletal protein 4.1R affects repolarization and regulates calcium handling in the heartMark A Stagg
Heart Science Centre, National Heart and Lung Institute, Imperial College London, United Kingdom
Circ Res 103:855-63. 2008..1R in modulating the functional properties of several cardiac ion transporters with consequences on cardiac electrophysiology and with possible significant roles during normal cardiac function and disease...
- Targeted deletion of alpha-adducin results in absent beta- and gamma-adducin, compensated hemolytic anemia, and lethal hydrocephalus in miceRaymond F Robledo
The Jackson Laboratory, Bar Harbor, ME, USA
Blood 112:4298-307. 2008..These data indicate that adducin plays a role in RBC membrane stability and in cerebrospinal fluid homeostasis...
- Protein 4.1R-dependent multiprotein complex: new insights into the structural organization of the red blood cell membraneMarcela Salomao
Red Cell Physiology Laboratory and Membrane Biochemistry Laboratory, New York Blood Center, New York, NY 10065, USA
Proc Natl Acad Sci U S A 105:8026-31. 2008....
- Protein 4.1R links E-cadherin/beta-catenin complex to the cytoskeleton through its direct interaction with beta-catenin and modulates adherens junction integrityShaomin Yang
Red Cell Physiology Laboratory, New York Blood Center, 310 East 67th St, New York, NY 10065, USA
Biochim Biophys Acta 1788:1458-65. 2009..1R in linking the cadherin/catenin complex to the cytoskeleton through its direct interaction with beta-catenin and in regulating the integrity of adherens junction...
- Coupled transcription-splicing regulation of mutually exclusive splicing events at the 5' exons of protein 4.1R geneShu Ching Huang
Department of Medical Oncology, Dana Farber Cancer Institute, Boston, MA 02115, USA
Blood 114:4233-42. 2009..Taken together, our results suggest that 4.1R gene expression involves transcriptional regulation coupled with a complex splicing regulatory network...
- Protein 4.1 expression in the developing hair cells of the mouse inner earKazuhiro Okumura
Department of Bioproduction, Tokyo University of Agriculture, 196, Yasaka, Abashiri, Hokkaido 099 2493, Japan
Brain Res 1307:53-62. 2010..1 family members play important roles in the development and maintenance of the inner ear hair cells, and that 4.1B may be a member of the myosin XV-whirlin complex that is important for stereocilia maturation...
- Hereditary spherocytosis and hereditary elliptocytosis: aberrant protein sorting during erythroblast enucleationMarcela Salomao
The Red Cell Physiology Laboratory, The New York Blood Center, New York, NY, USA
Blood 116:267-9. 2010..We conclude that aberrant protein sorting is one mechanistic basis for protein deficiencies in HE and HS...
- The Mediator complex protein Med31 is required for embryonic growth and cell proliferation during mammalian developmentMichael D Risley
University of Manchester, Faculty of Life Sciences, Manchester, UK
Dev Biol 342:146-56. 2010..As the Mediator complex is a transcriptional co-activator, our results suggest that Med31 functions to promote the transcription of genes required for embryonic growth and cell proliferation...
- β8 integrin and band 4.1B cooperatively regulate morphogenesis of the embryonic heartYoungsin Jung
Department of Cancer Biology, University of Texas M D Anderson Cancer Center, Houston, Texas 77030, USA
Dev Dyn 240:271-7. 2011..These data are the first to identify cell adhesion and signaling pathways regulated by αvβ8 integrin and Band 4.1B as essential for normal formation and function of the heart during embryogenesis...
- Lack of protein 4.1G causes altered expression and localization of the cell adhesion molecule nectin-like 4 in testis and can cause male infertilityShaomin Yang
Red Cell Physiology Laboratory, New York Blood Center, New York, New York 10065, USA
Mol Cell Biol 31:2276-86. 2011..Additionally, the finding that infertility is present in B6-129 but not on the B6 background suggests the presence of a major modifier gene(s) that influences 4.1G function and is associated with male infertility...
- Genomic structure of the locus encoding protein 4.1. Structural basis for complex combinational patterns of tissue-specific alternative RNA splicingJ P Huang
Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan, Republic of China
J Biol Chem 268:3758-66. 1993..1 isoform (135 kDa) that is predominantly expressed in nonerythroid tissues. Combinatorial splicing of these exons may generate different isoforms that exhibit complicated tissue-specific expression patterns...
- Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulinCatherine Creppe
GIGA Signal Transduction, University of Liege, C H U Sart Tilman, 4000 Liege, Belgium
Cell 136:551-64. 2009..Indeed, silencing of its scaffold (Elp1) or catalytic subunit (Elp3) cell-autonomously delays the migration and impairs the branching of projection neurons...
- Effect of complete protein 4.1R deficiency on ion transport properties of murine erythrocytesAlicia Rivera
Children s Hospital Boston, Dept of Laboratory Medicine, Harvard Medical School, Boston, MA 02115, USA
Am J Physiol Cell Physiol 291:C880-6. 2006..1 plays a major role in volume regulation and physiologically downregulates Na/H exchange in mouse erythrocytes. Upregulation of the Na/H exchange is an important contributor to the elevated cell Na content of 4.1(-/-) erythrocytes...
- Sequence, structure and chromosomal localization of Crtm gene encoding mouse cartilage matrix protein and its exclusion as a candidate for murine achondroplasiaA Aszodi
Department of Experimental Pathology, University Hospital, Lund, Sweden
Matrix Biol 16:563-73. 1998..Immunostaining for CMP and sequence of Crtm in cn/cn mice failed to reveal any disease-specific mutations, suggesting that mutations in Crtm do not cause achondroplasia...
- Characterization and chromosomal localization of PTPRO, a novel receptor protein tyrosine phosphatase, expressed in hematopoietic stem cellsS Avraham
Division of Experimental Medicine, Beth Israel Deaconess Medical Center, Harvard Institutes of Medicine, Boston, MA 02115, USA
Gene 204:5-16. 1997..The mouse Ptpro gene was mapped to chromosome 4, closely linked to D4Mit16 and Elp1 (elliptocytosis-1), by using genomic DNAs from a (C57BL/6J x Mus spretus)F1 x Mus spretus backcross...
- Genetic linkage of IgG autoantibody production in relation to lupus nephritis in New Zealand hybrid miceT J Vyse
Department of Pediatrics, National Jewish Center for Immunology and Respiratory Medicine, Denver, Colorado 80206, USA
J Clin Invest 98:1762-72. 1996..Interestingly, a distal chromosome 4 locus, Nba1, was linked with nephritis but not with any of the autoantibodies measured, suggesting that it contributes to renal disease at a checkpoint distal to autoantibody production...
- ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestrationR D Palmiter
Howard Hughes Medical Institute, University of Washington, Seattle 98195 7370, USA
EMBO J 15:1784-91. 1996..Prolonged exposure of cells expressing ZnT-2 to zinc causes an accretion of intracellular vesicles. We suggest that ZnT-2 protects these cells from zinc toxicity by facilitating zinc transport into an endosomal/lysosomal compartment...
- Asynchronous regulation of splicing events within protein 4.1 pre-mRNA during erythroid differentiationF Baklouti
Department of Internal Medicine, Boyer Center for Molecular Medicine, School of Medicine, Yale University, New Haven, CT
Blood 87:3934-41. 1996..These findings also show that the splicing of exon 16 alters the intracellular localization of protein 4.1 in MEL cells, and appears to be essential for its targeting to the plasmalemma...
- Genetic analysis of the NZB contribution to lupus-like autoimmune disease in (NZB x NZW)F1 miceC G Drake
Department of Pediatrics, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206
Proc Natl Acad Sci U S A 91:4062-6. 1994..It is of interest that a gene encoding a receptor for tumor necrosis factor maps to the vicinity of this disease-associated gene...
- Structural diversity of band 4.1 superfamily membersK Takeuchi
Department of Information Physiology, National Institute for Physiological Sciences, Aichi, Japan
J Cell Sci 107:1921-8. 1994..In this study, we describe the initial characterization of these new members and discuss the evolution of the band 4.1 superfamily...
- Evolutionarily conserved alternative pre-mRNA splicing regulates structure and function of the spectrin-actin binding domain of erythroid protein 4.1R Winardi
Life Sciences Division, Lawrence Berkeley National Laboratory, University of California 94720, USA
Blood 86:4315-22. 1995..Moreover, both nucleated amphibian erythrocytes and their enucleated mammalian counterparts express 4.1 isoforms functionally competent for spectrin-actin binding...
- Molecular basis of hereditary elliptocytosis due to protein 4.1 deficiencyJ Conboy
N Engl J Med 315:680-5. 1986..The chromosomal location of the gene that codes for protein 4.1 suggests that hereditary elliptocytosis in one class of patients with the disorder may be caused by a mutation of this gene...
- Neurobehavioral deficits in mice lacking the erythrocyte membrane cytoskeletal protein 4.1L D Walensky
Department of Neuroscience The Johns Hopkins School of Medicine Baltimore, Maryland 21205, USA
Curr Biol 8:1269-72. 1998..The neurobehavioral findings are consistent with the distribution of 4.1R in the brain, suggesting that 4.1R performs specific functions in the central nervous system...
- Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeletonJ Conboy
Proc Natl Acad Sci U S A 83:9512-6. 1986..1. The availability of cloned erythrocyte protein 4.1 cDNA should facilitate the study of the functional characteristics of this protein in erythroid as well as non-erythroid cells...
- Protein 4.1R-deficient mice are viable but have erythroid membrane skeleton abnormalitiesZ T Shi
Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA
J Clin Invest 103:331-40. 1999..1R expression is widespread among nonerythroid cells. The 4.1R knockout mice represent a valuable animal model for exploring 4.1R function in nonerythroid cells and for determining pathophysiological sequelae to 4.1R deficiency...
- A nonerythroid isoform of protein 4.1R interacts with components of the contractile apparatus in skeletal myofibersA Kontrogianni-Konstantopoulos
Department of Medicine, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Mol Biol Cell 11:3805-17. 2000..All of these observations suggest a topological model whereby 4.1R may play a scaffolding role by anchoring the actomyosin myofilaments and possibly modulating their displacements during contraction/relaxation...
- The prototypical 4.1R-10-kDa domain and the 4.1g-10-kDa paralog mediate fodrin-actin complex formationA Kontrogianni-Konstantopoulos
Department of Medicine, The Johns Hopkins University School of Medicine, University, Baltimore, Maryland 21205, USA
J Biol Chem 276:20679-87. 2001..1G are distributed underneath the plasma membrane in PC12 cells. Collectively, these observations suggest that brain 4.1R and 4.1G may modulate the membrane mechanical properties of neuronal cells by promoting fodrin/actin association...
- Decrease in hnRNP A/B expression during erythropoiesis mediates a pre-mRNA splicing switchVictor C Hou
Life Sciences Division, Lawrence Berkeley National Laboratory, University of California at Berkeley, Berkeley, CA 94720, USA
EMBO J 21:6195-204. 2002..These findings demonstrate that natural developmental changes in hnRNP A/B proteins can effect physiologically important switches in pre-mRNA splicing...
- Quantitative trait loci for baseline erythroid traitsLuanne L Peters
The Jackson Laboratory, 600 Main Street, Bar Harbor, Maine 04609, USA
Mamm Genome 17:298-309. 2006..These analyses emphasize the genetic complexity underlying the regulation of erythroid peripheral blood traits in normal populations and suggest that genes not previously recognized as significantly impacting normal erythropoiesis exist...
- Alternative 5' exons and differential splicing regulate expression of protein 4.1R isoforms with distinct N-terminiMarilyn K Parra
Lawrence Berkeley National Laboratory, Life Sciences Division, Berkeley, CA 94720, USA
Blood 101:4164-71. 2003..1R protein isoforms in various cell types is regulated by a novel mechanism requiring coordination between upstream transcription initiation events and downstream alternative splicing events...
- Cardiac muscle cell cytoskeletal protein 4.1: analysis of transcripts and subcellular location--relevance to membrane integrity, microstructure, and possible role in heart failurePamela M Taylor-Harris
Randall Division of Cell and Molecular Biophysics, King s College London, Guy s Campus, London SE1 1UL, UK
Mamm Genome 16:137-51. 2005..Four genes, EPB41, EPB41L1, EPB41L2, and EPB41L3 encode proteins 4.1R, 4.1N, 4.1G, and 4.1B, respectively...
- Evidence for a protective role of the Gardos channel against hemolysis in murine spherocytosisLucia De Franceschi
Department of Clinical and Experimental Medicine, Section of Internal Medicine, University of Verona, Italy
Blood 106:1454-9. 2005....
- Genetic loci affecting body weight and fatness in a C57BL/6J x PWK/PhJ mouse intercrossHongguang Shao
Monell Chemical Senses Center, 3500 Market Street, Philadelphia, Pennsylvania 19104, USA
Mamm Genome 18:839-51. 2007..The location and type of QTLs detected in this new cross will assist in future efforts to identify the genetic variation that determines the ratio of lean to fat weight as well as body size in mice...
- Four paralogous protein 4.1 genes map to distinct chromosomes in mouse and humanL L Peters
The Jackson Laboratory, Bar Harbor, Maine, 04609, USA
Genomics 54:348-50. 1998..In addition to the prototypical red blood cell 4.1R (human gene symbol EPB41,) these include two homologues that are strongly expressed in the brain (4.1N, EPB41L1; and 4...
- GENETIC INTERACTIONS IN RED CELL MEMBRANE DISEASELUANNE PETERS; Fiscal Year: 2003....
- CHANNEL-MEDIATED RBC DEHYDRATION IN SICKLE CELL DISEASEAlicia Rivera; Fiscal Year: 2003..It is additionally significant, because it will provide the means for the applicant to establish an independent research career and to become competitive for a tenure-track assistant professional position. ..
- Hemolytic Anemia: ModelsLUANNE PETERS; Fiscal Year: 2006..5 isoform in the structure and assembly of the sarcoplasmic reticulum by an in vivo developmental study. ..
- Cytokines in Sickle Cell Volume RegulationAlicia Rivera; Fiscal Year: 2006..abstract_text> ..
- Adducin and the Membrane SkeletonLUANNE PETERS; Fiscal Year: 2007..Follow up studies will include electrocardiology and echocardiology. ..
- Mouse Models for Heart, Lung and Blood DiseaseLUANNE PETERS; Fiscal Year: 2007..New mouse models will be cryo-preserved in order to maintain their availability. Provision are likewise to maintain all JAX PGA resources beyond the PGA program. ..
- RED CELL CYTOSKELETAL PROTEIN AND MITOSISShu Ching Huang; Fiscal Year: 2008..Finally, we shall define the relationship between changes in the expression of these 4.1R isoforms and the transition from proliferation to post-mitotic states during erythroid differentiation. ..
- ORGANELLE MEMBRANES IN PLATELET STORAGE POOL DISEASELUANNE PETERS; Fiscal Year: 2009..Lung fibrosis typically leads to death in the 4th to 5th decades. This study is designed to identify the underlying genetic causes of HPS, which will provide avenues of research for potential therapies. ..