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Bicaudal D

BicD, Bicaudal-D, BICD1
This gene is one of two human homologs of Drosophila bicaudal-D. It has been implicated in COPI-independent membrane transport from the Golgi apparatus to the endoplasmic reticulum. Two alternative splice variants have been described. Other alternative splice variants that encode different protein isoforms have been described but their full-length nature has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Rab6, CAN, OUT, Rab5, dynactin
Papers on BicD
Phenotypic characterisation of RAB6A knockout mouse embryonic fibroblasts.
Goud et al., Paris, France. In Biol Cell, Dec 2015
We show that Rab6 depletion affects cell growth, alters Golgi morphology and decreases the Golgi-associated levels of some known Rab6 effectors such as Bicaudal-D and myosin II.
Reconstitution of the targeting of Rab6A to the Golgi apparatus in semi-intact HeLa cells: A role of BICD2 in stabilizing Rab6A on Golgi membranes and a concerted role of Rab6A/BICD2 interactions in Golgi-to-ER retrograde transport.
Murata et al., Tokyo, Japan. In Biochim Biophys Acta, Oct 2015
Golgi-targeting assays identified Bicaudal-D (BICD)2, which is reportedly involved in the dynein-mediated transport of mRNAs during oogenesis and embryogenesis in Drosophila, as a cytosolic factor for the Golgi targeting of Rab6A in SLO-permeabilized HeLa cells.
Structural basis for cargo binding and autoinhibition of Bicaudal-D1 by a parallel coiled-coil with homotypic registry.
Wakamatsu et al., Kiryū, Japan. In Biochem Biophys Res Commun, Jun 2015
The crystal structure of BICD1 CC3 revealed a parallel homodimeric coiled-coil with asymmetry and complementary knobs-into-holes interactions, differing from Drosophila BicD CC3.
The role of Rab6 GTPase in the maturation of phagosome against Staphylococcus aureus.
Zhang et al., Hangzhou, China. In Int J Biochem Cell Biol, Apr 2015
It was revealed that Rab6 GTPase was required during the phagosome maturation by its interaction with bicaudal-D1 (BICD1) protein.
hTERT, BICD1 and chromosome 18 polymorphisms associated with telomere length affect kidney allograft function after transplantation.
Ciechanowski et al., Szczecin, Poland. In Kidney Blood Press Res, 2014
The aim of this study was to analyse the associations between graft rs2735940 hTERT and rs2630578 BICD1 gene polymorphisms and rs7235755/rs2162440 chromosome 18 polymorphisms, relative TL and kidney function after transplantation.
Phenotypic and genetic heterogeneity among subjects with mild airflow obstruction in COPDGene.
COPDGene Investigators et al., Boston, United States. In Respir Med, 2014
The emphysema-predominant GOLD 1 cluster was nominally associated with rs7671167 (FAM13A) and rs161976 (BICD1).
Bicaudal d family adaptor proteins control the velocity of Dynein-based movements.
Hoogenraad et al., Rotterdam, Netherlands. In Cell Rep, 2014
We also find that Bicaudal D (BICD) adaptor proteins can regulate dynein-based vesicle motility.
Genetics of COPD.
Nakamura, Tokyo, Japan. In Allergol Int, 2011
Another GWA study has shown that BICD1 in 12p11 was associated with the presence or absence of emphysema.
Genome-wide association study identifies BICD1 as a susceptibility gene for emphysema.
ECLIPSE Study NETT Investigators et al., King of Prussia, United States. In Am J Respir Crit Care Med, 2011
Variants in BICD1 are associated with length of telomeres, which suggests that a mechanism linked to accelerated aging may be involved in the pathogenesis of emphysema.
A novel protease-activated receptor-1 interactor, Bicaudal D1, regulates G protein signaling and internalization.
Kuliopulos et al., Boston, United States. In J Biol Chem, 2010
the protease-activated receptor-1 interactor, Bicaudal D1, regulates G protein signaling and internalization
Bicaudal-D binds clathrin heavy chain to promote its transport and augments synaptic vesicle recycling.
Bullock et al., Cambridge, United Kingdom. In Embo J, 2010
Results implicate BicD as a new player in clathrin-associated trafficking processes and show a novel requirement for microtubule-based motor transport in the synaptic vesicle cycle.
Dynein and kinesin regulate stress-granule and P-body dynamics.
Boccaccio et al., Buenos Aires, Argentina. In J Cell Sci, 2009
Impairment of retrograde transport by knockdown of DHC1 or BicD1 inhibits stress-granule formation and P-body growth upon stress.
Bicaudal-D and its role in cargo sorting by microtubule-based motors.
Li et al., Cambridge, United Kingdom. In Biochem Soc Trans, 2009
In the present review, we concentrate on the BicD (Bicaudal-D) protein, which has recently emerged as an essential element for transport of several important cargoes by the minus-end-directed motor cytoplasmic dynein.
BicaudalD actively regulates microtubule motor activity in lipid droplet transport.
Gross et al., Irvine, United States. In Plos One, 2007
while BicD might contribute to recruitment of dynein to the cargo it is not absolutely required for such dynein localization
Golgins and GTPases, giving identity and structure to the Golgi apparatus.
Barr et al., Martinsried, Germany. In Biochim Biophys Acta, 2005
Similarly, other golgins such as the vesicle tethering factor p115 and Bicaudal-D are targeted by the Rab GTPases, Rab1 and Rab6, respectively.
Egalitarian binds dynein light chain to establish oocyte polarity and maintain oocyte fate.
Lehmann et al., New York City, United States. In Nat Cell Biol, 2004
In Drosophila melanogaster, the Egalitarian (Egl) and Bicaudal-D (BicD) proteins are also essential for the transport of macromolecules to the oocyte and to the apical surface of the blastoderm embryo.
Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complex.
Hoogenraad et al., Münster, Germany. In Nat Cell Biol, 2002
In particular, we identified the dynein-dynactin-binding protein Bicaudal-D1 (BICD1), one of the two mammalian homologues of Drosophila Bicaudal-D.
Drosophila Lissencephaly-1 functions with Bic-D and dynein in oocyte determination and nuclear positioning.
Suter et al., Montréal, Canada. In Nat Cell Biol, 1999
Here we show that the Drosophila homologue of Lissencephaly-1, DLis-1, acts together with Bicaudal-D (Bic-D), Egalitarian (Egl), dynein and microtubules to determine oocyte identity.
Requirement for phosphorylation and localization of the Bicaudal-D protein in Drosophila oocyte differentiation.
Steward et al., Princeton, United States. In Cell, 1991
Bic-D is required for the differentiation of an oocyte and hence for fertility.
Structure of the Drosophila BicaudalD protein and its role in localizing the the posterior determinant nanos.
Struhl et al., New York City, United States. In Cell, 1990
Mutations in the BicaudalD (BicD) gene lead to a global reorganization of the Drosophila body pattern such that the head, thoracic, and anterior abdominal segments are replaced by posterior abdominal segments and terminalia.
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