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XBX-1 encodes a dynein light intermediate chain required for retrograde intraflagellar transport and cilia assembly in Caenorhabditis elegans.
Schafer JC, Haycraft CJ, Thomas JH, Yoder BK, Swoboda P
(2003) Mol Biol Cell 14: 2057-70
MeSH Terms: Animals, Animals, Genetically Modified, Caenorhabditis elegans, Cilia, Dyneins, Flagella, Gene Expression Regulation, Genes, Reporter, Molecular Motor Proteins, Sequence Deletion
Show Abstract · Added January 20, 2015
Intraflagellar transport (IFT) is a process required for flagella and cilia assembly that describes the dynein and kinesin mediated movement of particles along axonemes that consists of an A and a B complex, defects in which disrupt retrograde and anterograde transport, respectively. Herein, we describe a novel Caenorhabditis elegans gene, xbx-1, that is required for retrograde IFT and shares homology with a mammalian dynein light intermediate chain (D2LIC). xbx-1 expression in ciliated sensory neurons is regulated by the transcription factor DAF-19, as demonstrated previously for genes encoding IFT complex B proteins. XBX-1 localizes to the base of the cilia and undergoes anterograde and retrograde movement along the axoneme. Disruption of xbx-1 results in cilia defects and causes behavioral abnormalities observed in other cilia mutants. Analysis of cilia in xbx-1 mutants reveals that they are shortened and have a bulb like structure in which IFT proteins accumulate. The role of XBX-1 in IFT was further confirmed by analyzing the effect that other IFT mutations have on XBX-1 localization and movement. In contrast to other IFT proteins, retrograde XBX-1 movement was detected in complex A mutants. Our results suggest that the DLIC protein XBX-1 functions together with the CHE-3 dynein in retrograde IFT, downstream of the complex A proteins.
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10 MeSH Terms
The betagamma subunit of heterotrimeric G proteins interacts with RACK1 and two other WD repeat proteins.
Dell EJ, Connor J, Chen S, Stebbins EG, Skiba NP, Mochly-Rosen D, Hamm HE
(2002) J Biol Chem 277: 49888-95
MeSH Terms: 3T3 Cells, Amino Acid Motifs, Amino Acid Sequence, Animals, Binding Sites, Blotting, Western, Cytoplasm, DNA Mutational Analysis, Dimerization, Dose-Response Relationship, Drug, Dynamin I, Dyneins, GTP-Binding Proteins, Glutathione Transferase, Heterotrimeric GTP-Binding Proteins, Humans, Isoenzymes, Mice, Models, Molecular, Molecular Sequence Data, Mutation, Neoplasm Proteins, Precipitin Tests, Protein Binding, Protein Kinase C, Protein Kinase C beta, Protein Structure, Secondary, Protein Structure, Tertiary, Receptors for Activated C Kinase, Receptors, Cell Surface, Sequence Homology, Amino Acid, Signal Transduction, Two-Hybrid System Techniques
Show Abstract · Added December 10, 2013
A yeast two-hybrid approach was used to discern possible new effectors for the betagamma subunit of heterotrimeric G proteins. Three of the clones isolated are structurally similar to Gbeta, each exhibiting the WD40 repeat motif. Two of these proteins, the receptor for activated C kinase 1 (RACK1) and the dynein intermediate chain, co-immunoprecipitate with Gbetagamma using an anti-Gbeta antibody. The third protein, AAH20044, has no known function; however, sequence analysis indicates that it is a WD40 repeat protein. Further investigation with RACK1 shows that it not only interacts with Gbeta(1)gamma(1) but also unexpectedly with the transducin heterotrimer Galpha(t)beta(1)gamma(1). Galpha(t) alone does not interact, but it must contribute to the interaction because the apparent EC(50) value of RACK1 for Galpha(t)beta(1)gamma(1) is 3-fold greater than that for Gbeta(1)gamma(1) (0.1 versus 0.3 microm). RACK1 is a scaffold that interacts with several proteins, among which are activated betaIIPKC and dynamin-1 (1). betaIIPKC and dynamin-1 compete with Gbeta(1)gamma(1) and Galpha(t)beta(1)gamma(1) for interaction with RACK1. These findings have several implications: 1) that WD40 repeat proteins may interact with each other; 2) that Gbetagamma interacts differently with RACK1 than with its other known effectors; and/or 3) that the G protein-RACK1 complex may constitute a signaling scaffold important for intracellular responses.
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33 MeSH Terms
Targeted mutation of Cyln2 in the Williams syndrome critical region links CLIP-115 haploinsufficiency to neurodevelopmental abnormalities in mice.
Hoogenraad CC, Koekkoek B, Akhmanova A, Krugers H, Dortland B, Miedema M, van Alphen A, Kistler WM, Jaegle M, Koutsourakis M, Van Camp N, Verhoye M, van der Linden A, Kaverina I, Grosveld F, De Zeeuw CI, Galjart N
(2002) Nat Genet 32: 116-27
MeSH Terms: Animals, Brain, Dynactin Complex, Dyneins, Gene Targeting, Heterozygote, Mice, Mice, Knockout, Microtubule-Associated Proteins, Motor Activity, Mutagenesis, Site-Directed, Neoplasm Proteins, Nerve Tissue Proteins, Phenotype, Williams Syndrome
Show Abstract · Added December 10, 2013
Williams syndrome is a neurodevelopmental disorder caused by the hemizygous deletion of 1.6 Mb on human chromosome 7q11.23. This region comprises the gene CYLN2, encoding CLIP-115, a microtubule-binding protein of 115 kD. Using a gene-targeting approach, we provide evidence that mice with haploinsufficiency for Cyln2 have features reminiscent of Williams syndrome, including mild growth deficiency, brain abnormalities, hippocampal dysfunction and particular deficits in motor coordination. Absence of CLIP-115 also leads to increased levels of CLIP-170 (a closely related cytoplasmic linker protein) and dynactin at the tips of growing microtubules. This protein redistribution may affect dynein motor regulation and, together with the loss of CLIP-115-specific functions, underlie neurological alterations in Williams syndrome.
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15 MeSH Terms
Modulation of substrate adhesion dynamics via microtubule targeting requires kinesin-1.
Krylyshkina O, Kaverina I, Kranewitter W, Steffen W, Alonso MC, Cross RA, Small JV
(2002) J Cell Biol 156: 349-59
MeSH Terms: Animals, Cell Line, Cell Movement, Dyneins, Fibroblasts, Focal Adhesions, Humans, Kinesin, Membrane Glycoproteins, Membrane Potentials, Mice, Microscopy, Video, Microtubules, Molecular Motor Proteins, Mutagenesis, Nocodazole, Polymerase Chain Reaction, Protein Binding, Rats, Xenopus
Show Abstract · Added December 10, 2013
Recent studies have shown that the targeting of substrate adhesions by microtubules promotes adhesion site disassembly (Kaverina, I., O. Krylyshkina, and J.V. Small. 1999. J. Cell Biol. 146:1033-1043). It was accordingly suggested that microtubules serve to convey a signal to adhesion sites to modulate their turnover. Because microtubule motors would be the most likely candidates for effecting signal transmission, we have investigated the consequence of blocking microtubule motor activity on adhesion site dynamics. Using a function-blocking antibody as well as dynamitin overexpression, we found that a block in dynein-cargo interaction induced no change in adhesion site dynamics in Xenopus fibroblasts. In comparison, a block of kinesin-1 activity, either via microinjection of the SUK-4 antibody or of a kinesin-1 heavy chain construct mutated in the motor domain, induced a dramatic increase in the size and reduction in number of substrate adhesions, mimicking the effect observed after microtubule disruption by nocodazole. Blockage of kinesin activity had no influence on either the ability of microtubules to target substrate adhesions or on microtubule polymerisation dynamics. We conclude that conventional kinesin is not required for the guidance of microtubules into substrate adhesions, but is required for the focal delivery of a component(s) that retards their growth or promotes their disassembly.
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20 MeSH Terms
Drosophila roadblock and Chlamydomonas LC7: a conserved family of dynein-associated proteins involved in axonal transport, flagellar motility, and mitosis.
Bowman AB, Patel-King RS, Benashski SE, McCaffery JM, Goldstein LS, King SM
(1999) J Cell Biol 146: 165-80
MeSH Terms: Amino Acid Sequence, Animals, Axonal Transport, Carrier Proteins, Chlamydomonas, Cloning, Molecular, Conserved Sequence, Drosophila Proteins, Drosophila melanogaster, Dyneins, Female, Flagella, Genes, Insect, Microscopy, Electron, Mitosis, Molecular Sequence Data, Mutation, Phylogeny, Plant Proteins, Protozoan Proteins, Reproduction, Sequence Alignment
Show Abstract · Added June 9, 2010
Eukaryotic organisms utilize microtubule-dependent motors of the kinesin and dynein superfamilies to generate intracellular movement. To identify new genes involved in the regulation of axonal transport in Drosophila melanogaster, we undertook a screen based upon the sluggish larval phenotype of known motor mutants. One of the mutants identified in this screen, roadblock (robl), exhibits diverse defects in intracellular transport including axonal transport and mitosis. These defects include intra-axonal accumulations of cargoes, severe axonal degeneration, and aberrant chromosome segregation. The gene identified by robl encodes a 97-amino acid polypeptide that is 57% identical (70% similar) to the 105-amino acid Chlamydomonas outer arm dynein-associated protein LC7, also reported here. Both robl and LC7 have homology to several other genes from fruit fly, nematode, and mammals, but not Saccharomyces cerevisiae. Furthermore, we demonstrate that members of this family of proteins are associated with both flagellar outer arm dynein and Drosophila and rat brain cytoplasmic dynein. We propose that roadblock/LC7 family members may modulate specific dynein functions.
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22 MeSH Terms
Functional design in the actin cytoskeleton.
Small JV, Rottner K, Kaverina I
(1999) Curr Opin Cell Biol 11: 54-60
MeSH Terms: Actins, Animals, Biological Transport, Cell Adhesion, Cell Line, Cell Movement, Cell Polarity, Cell Size, Cytoskeleton, Dyneins, GTP-Binding Proteins, Kinesin, Membrane Proteins, Microtubules, Models, Biological, Myosins, rac GTP-Binding Proteins, rhoB GTP-Binding Protein
Show Abstract · Added December 10, 2013
Changes in cell shape, anchorage and motility are all associated with the dynamic reorganisation of the architectural arrays of actin filaments that make up the actin cytoskeleton. The relative expression of these functionally different actin filament arrays is intimately linked to the pattern of contacts that a cell develops with its extracellular substrate. Cell polarity is acquired by the development of an asymmetric pattern of substrate contacts, effected in a specific, site-directed manner by the delivery of adhesion-site modulators along microtubules.
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18 MeSH Terms
Sertoli cell processes have axoplasmic features: an ordered microtubule distribution and an abundant high molecular weight microtubule-associated protein (cytoplasmic dynein).
Neely MD, Boekelheide K
(1988) J Cell Biol 107: 1767-76
MeSH Terms: Adenosine Triphosphatases, Animals, Brain, Cytoplasm, Dyneins, Electrophoresis, Polyacrylamide Gel, Hot Temperature, Male, Microtubule-Associated Proteins, Microtubules, Molecular Weight, Rats, Sertoli Cells, Testis
Show Abstract · Added September 13, 2014
Microtubules in the cytoplasm of rat Sertoli cell stage VI-VIII testicular seminiferous epithelium were studied morphometrically by electron microscopy. The Sertoli cell microtubules demonstrated axonal features, being largely parallel in orientation and predominantly spaced one to two microtubule diameters apart, suggesting the presence of microtubule-bound spacer molecules. Testis microtubule-associated proteins (MAPs) were isolated by a taxol, salt elution procedure. Testis MAPs promoted microtubule assembly, but to a lesser degree than brain MAPs. High molecular weight MAPs, similar in electrophoretic mobilities to brain MAP-1 and MAP-2, were prominent components of total testis MAPs, though no shared immunoreactivity was detected between testis and brain high molecular weight MAPs using both polyclonal and monoclonal antibodies. Unlike brain high molecular weight MAPs, testis high molecular weight MAPs were not heat stable. Testis MAP composition, studied on postnatal days 5, 10, 15, and 24 and in the adult, changed dramatically during ontogeny. However, the expression of the major testis high molecular weight MAP, called HMW-2, was constitutive and independent of the development of mature germ cells. The Sertoli cell origin of HMW-2 was confirmed by identifying this protein as the major MAP found in an enriched Sertoli cell preparation and in two rat models of testicular injury characterized by germ cell depletion. HMW-2 was selectively released from testis microtubules by ATP and co-purified by sucrose density gradient centrifugation with MAP-1C, a neuronal cytoplasmic dynein. The inhibition of the microtubule-activated ATPase activity of HMW-2 by vanadate and erythro-(2-hydroxy-3-nonyl)adenine and its proteolytic breakdown by vanadate-dependent UV photocleavage confirmed the dynein-like nature of HMW-2. As demonstrated by this study, the neuronal and Sertoli cell cytoskeletons share morphological, structural and functional properties.
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14 MeSH Terms
HMW-2, the Sertoli cell cytoplasmic dynein from rat testis, is a dimer composed of nearly identical subunits.
Neely MD, Erickson HP, Boekelheide K
(1990) J Biol Chem 265: 8691-8
MeSH Terms: Adenosine Triphosphatases, Animals, Cytoplasm, Dyneins, Macromolecular Substances, Male, Microscopy, Electron, Molecular Weight, Rats, Sertoli Cells
Show Abstract · Added September 13, 2014
The ultrastructure and biochemical characteristics of HMW-2, the Sertoli cell cytoplasmic dynein isolated from rat testes, were analyzed. Electron microscopic studies revealed a two-headed two-stem structure with dimensions very similar to other dyneins. We found that, like other cytoplasmic dyneins, both heads have an approximately spherical shape with a central cavity. Heavy chain analysis suggested the presence of only one type of heavy chain, a finding that was supported by the simple Michaelis-Menten kinetics displayed by the HMW-2-associated ATPase activity. In addition, dissociation of the HMW-2 complex resulted in a single type of dynein subunit sedimenting at 11.8 S. This fraction contained all the polypeptides present in the undissociated HMW-2. Ultrastructurally the HMW-2 subunits were composed of one globular domain with a tail. The simplest interpretation is that HMW-2 is a dimer of nearly identical subunits, each containing one heavy chain, one 90-kDa intermediate chain, and two light chains.
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10 MeSH Terms