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Genomes and Genes | S M KingSummaryAffiliation: University of Connecticut Health Center Country: USA Publications
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Dyneins motor on in plantsStephen M King
Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, Connecticut 06030 3305, USA
Traffic 3:930-1. 2002..These observations also suggest that, in contrast to an earlier proposal, flowering plants may indeed use standard dynein-driven mechanisms to perform cellular transport activities that, in other organisms, employ the dynein motor..- Axonemal protofilament ribbons, DM10 domains, and the link to juvenile myoclonic epilepsyStephen M King
Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, Connecticut, USA
Cell Motil Cytoskeleton 63:245-53. 2006..Here I discuss recent work that supports assignment of human Efhc1 as a ciliary component and the resulting implications for the mechanism of disease causation... - AAA domains and organization of the dynein motor unitS M King
Department of Biochemistry, University of Connecticut Health Center, Farmington, CT 06032 3305, USA
J Cell Sci 113:2521-6. 2000..The resulting structural parallels allow intriguing predictions to be made concerning dynein organization and motor function... - Cytoplasmic dynein contains a family of differentially expressed light chainsS M King
Department of Biochemistry, Center for Biomedical Imaging Technology, University of Connecticut Health Center, Farmington 06032 3305, USA
Biochemistry 37:15033-41. 1998..Dissection of the cytoplasmic dynein complex revealed that Tctex1, an Mr 8000 LC dimer, and IC74 associate to define a basal-located intermediate chain/light chain complex analogous to that found in flagellar outer arm dynein... - The Tctex1/Tctex2 class of dynein light chains. Dimerization, differential expression, and interaction with the LC8 protein familyL M DiBella
Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06030 3305, USA
J Biol Chem 276:14366-73. 2001..These data provide further support for the existence of functionally distinct populations of cytoplasmic dynein with differing light chain content... - Dynein motors of the Chlamydomonas flagellumL M DiBella
Department of Biochemistry, University of Connecticut Health Center, Farmington 06032, USA
Int Rev Cytol 210:227-68. 2001..The combination of genetic, physiological, structural, and biochemical approaches has made the Chlamydomonas flagellum a very powerful model system in which to dissect the function of these fascinating molecular motors... - The mouse t-complex-encoded protein Tctex-1 is a light chain of brain cytoplasmic dyneinS M King
Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06032 3305, USA
J Biol Chem 271:32281-7. 1996.... 
Chlamydomonas outer arm dynein alters conformation in response to Ca2+Miho Sakato
Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030, USA
Mol Biol Cell 18:3620-34. 2007....- Chlamydomonas FAP133 is a dynein intermediate chain associated with the retrograde intraflagellar transport motorPanteleimon Rompolas
Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030, USA
J Cell Sci 120:3653-65. 2007..Furthermore, we found that FAP133, LC8, DHC1b, D1bLIC, the FLA10 kinesin-2 necessary for anterograde IFT and other IFT scaffold components associate to form a large macromolecular assembly... - Calcium regulates ATP-sensitive microtubule binding by Chlamydomonas outer arm dyneinMiho Sakato
Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06030-3305, USA
J Biol Chem 278:43571-9. 2003.... - Organization and regulation of the dynein microtubule motorStephen M King
Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030-3305, USA
Cell Biol Int 27:213-5. 2003 
Dynein-independent functions of DYNLL1/LC8: redox state sensing and transcriptional controlStephen M King
Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030 3305, USA
Sci Signal 1:pe51. 2008..A recent report now proposes that DYNLL/LC8-driven interactions are also regulated by changes in cellular redox state, which lead to intermonomer disulfide bond formation and ultimately activation of the transcription factor NF-kappaB...- Modulation of Chlamydomonas reinhardtii flagellar motility by redox poiseKen-ichi Wakabayashi
Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030, USA
J Cell Biol 173:743-54. 2006..These data indicate that redox poise directly affects ODAs and suggest that it may act in the control of flagellar motility... - Redox-based control of the gamma heavy chain ATPase from Chlamydomonas outer arm dyneinAlistair Harrison
Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06030-3305, USA
Cell Motil Cytoskeleton 52:131-43. 2002..These data suggest the possibility of a dynein-associated redox cascade and further support the idea that the gamma heavy chain plays a key regulatory role within the outer arm... - Sensing the mechanical state of the axoneme and integration of Ca2+ signaling by outer arm dyneinStephen M King
Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, Connecticut 06030 3305, USA
Cytoskeleton (Hoboken) 67:207-13. 2010.... - Flagellar radial spokes contain a Ca2+-stimulated nucleoside diphosphate kinaseRamila S Patel-King
Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, Connecticut 06030-3305, USA
Mol Biol Cell 15:3891-902. 2004..These observations suggest that nucleotides other than ATP may play an important role in the signal transduction pathway that underlies the regulatory mechanism defined by the radial spokes... - Brain cytoplasmic and flagellar outer arm dyneins share a highly conserved Mr 8,000 light chainS M King
Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06032 3305, USA
J Biol Chem 271:19358-66. 1996..Thus, it appears that flagellar outer arm and brain cytoplasmic dyneins share a highly conserved light chain polypeptide that, at least in Drosophila, is essential for viability... - The dynein microtubule motorS M King
Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06032 3305, USA
Biochim Biophys Acta 1496:60-75. 2000..Recent molecular, genetic and structural studies have revealed insight into the roles played by these various components and the mechanisms of dynein-based motility... - The LC7 light chains of Chlamydomonas flagellar dyneins interact with components required for both motor assembly and regulationLinda M DiBella
Department of Biochemistry, University of Connecticut Health Center, Farmington, CT 06030-3305, USA
Mol Biol Cell 15:4633-46. 2004..These data suggest that LC7a stabilizes both the outer arms and inner arm I1 and that both LC7a and LC7b are involved in multiple intradynein interactions within both dyneins... - The Roadblock light chains are ubiquitous components of cytoplasmic dynein that form homo- and heterodimersKarina Nikulina
Department of Biochemistry, University of Connecticut Health Center, Farmington 06030 3305, USA
Cell Motil Cytoskeleton 57:233-45. 2004..Immunofluorescence analysis reveals that Robl is present in punctate organelles in rat neuroblastoma cells. In testis, Robl is found in Leydig cells, spermatocytes, and sperm flagella... - Relaxation-based structure refinement and backbone molecular dynamics of the dynein motor domain-associated light chainHongwei Wu
Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, Connecticut 06030-3305, USA
Biochemistry 42:57-71. 2003..These results, which were cross validated using the 500 MHz data set, strongly support identification of the predicted LC1 binding surfaces and provide additional insight into the interaction mechanisms of leucine-rich repeat proteins... - An outer arm dynein light chain acts in a conformational switch for flagellar motilityRamila S Patel-King
Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030, USA
J Cell Biol 186:283-95. 2009..We propose that this gamma HC-LC1-microtubule ternary complex functions as a conformational switch to control outer arm activity... - Differential light chain assembly influences outer arm dynein motor functionLinda M DiBella
Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030-3305, USA
Mol Biol Cell 16:5661-74. 2005..These data suggest that LC2, LC6, and LC9 have different roles in outer arm assembly and are required for wild-type motor function in the Chlamydomonas flagellum... - A novel Tctex2-related light chain is required for stability of inner dynein arm I1 and motor function in the Chlamydomonas flagellumLinda M DiBella
Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030-3305, USA
J Biol Chem 279:21666-76. 2004..Furthermore, using a microtubule sliding assay we observed that dynein motor function is reduced in vitro. These data indicate that Tctex2b is required for the stability of inner dynein arm I1 and wild-type axonemal dynein function... - Three members of the LC8/DYNLL family are required for outer arm dynein motor functionChristopher A Tanner
Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030 3305, USA
Mol Biol Cell 19:3724-34. 2008..g., oda1). These results support a key regulatory role for the intermediate chain/light chain complex that is an integral and highly conserved feature of all oligomeric dynein motors... - A bipartite Ca2+-regulated nucleoside-diphosphate kinase system within the Chlamydomonas flagellum. The regulatory subunit p72Ramila S Patel-King
Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030 3305, USA
J Biol Chem 277:34271-9. 2002..We propose that Ca(2+) regulation of flagellar motility in Chlamydomonas may be achieved in part through a downstream GTP-mediated signaling pathway... - Backbone dynamics of dynein light chainsHongwei Wu
Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06030-3305, USA
Cell Motil Cytoskeleton 54:267-73. 2003 - Solution structure of the Tctex1 dimer reveals a mechanism for dynein-cargo interactionsHongwei Wu
Department of Molecular, Microbial, and Structural Biology, 263 Farmington Avenue, Farmington, Connecticut 06030, USA
Structure 13:213-23. 2005..In addition, this structure provides insight into the consequences of the mutations found in the t haplotype forms of this protein... - Purification of axonemal dyneins and dynein-associated components from ChlamydomonasStephen M King
Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, 06030 3305, USA
Methods Cell Biol 92:31-48. 2009..When combined with the wide range of available mutants, these methods allow for the analysis of dyneins lacking individual components or motor units... - Design and regulation of the AAA+ microtubule motor dyneinMiho Sakato
Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030-3305, USA
J Struct Biol 146:58-71. 2004..Here we describe the two basic dynein designs and detail the various regulatory systems that impinge on this motor within the eukaryotic flagellum... - Schmidtea mediterranea: a model system for analysis of motile ciliaPanteleimon Rompolas
Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, Connecticut 06030 3305, USA
Methods Cell Biol 93:81-98. 2009..mediterranea. Overall, S. mediterranea is a highly versatile, easy to maintain, and genetically tractable organism that provides a powerful alternative model system for the study of motile cilia... - The lissencephaly protein Lis1 is present in motile mammalian cilia and requires outer arm dynein for targeting to Chlamydomonas flagellaLotte B Pedersen
Department of Molecular Biology, University of Copenhagen, Universitetsparken 13, DK 2100 Copenhagen OE, Denmark
J Cell Sci 120:858-67. 2007..Our results suggest that Lis1 and NudC are present in cilia and flagella and may regulate outer dynein arm activity... - Genetic analysis of the cytoplasmic dynein subunit familiesK Kevin Pfister
Department of Cell Biology, School of Medicine, University of Virginia, Charlottesville, Virginia, USA
PLoS Genet 2:e1. 2006.... - Radial spoke proteins of Chlamydomonas flagellaPinfen Yang
Department of Biological Sciences, Marquette University, Milwaukee, WI 53233, USA
J Cell Sci 119:1165-74. 2006..The human genes encoding these proteins are candidates for causing primary ciliary dyskinesia, a severe inherited disease involving missing or defective axonemal structures, including the radial spokes... - Partially functional outer-arm dynein in a novel Chlamydomonas mutant expressing a truncated gamma heavy chainZhongmei Liu
Department of Biological Sciences, Graduate School of Science, University of Tokyo, 7 3 1 Hongo, Bunkyo ku, Tokyo 113 0033, Japan
Eukaryot Cell 7:1136-45. 2008..The availability of mutants lacking individual heavy chains should greatly facilitate studies on the structure and function of the outer-arm dynein... - Protein modification to probe intradynein interactions and in vivo redox stateKen Ichi Wakabayashi
Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan
Methods Mol Biol 392:71-83. 2007..Although designed for analysis of Chlamydomonas flagellar dyneins, these approaches should be readily adaptable to the study of other systems... - Molecular characterization of Ciona sperm outer arm dynein reveals multiple components related to outer arm docking complex protein 2Akiko Hozumi
Shimoda Marine Research Center, University of Tsukuba, Shizuoka, Japan
Cell Motil Cytoskeleton 63:591-603. 2006..Thus, the assembly of outer arm dynein onto doublet microtubules involves multiple coiled-coil proteins related to DC2... - Identification and analysis of axonemal dynein light chain 1 in primary ciliary dyskinesia patientsJudit Horvath
Department of Pediatrics and Adolescent Medicine, Albert Ludwigs University, Freiburg, Germany
Am J Respir Cell Mol Biol 33:41-7. 2005..Based on these findings, we considered DNAL1 a candidate for PCD and sequenced all exons of DNAL1 in 86 patients. Mutational analysis was negative, excluding a major role of DNAL1 in the pathogenesis of PCD... - Interaction of the DYNLT (TCTEX1/RP3) light chains and the intermediate chains reveals novel intersubunit regulation during assembly of the dynein complexKevin W H Lo
Department of Cell Biology, School of Medicine, University of Virginia, Charlottesville, Virginia 22908, USA
J Biol Chem 282:36871-8. 2007..Thus, whereas all combinations of DYNLT light chain dimers can be made, not all of the possible combinations of the isoforms are utilized during the assembly of the dynein complex... - Rab6 family proteins interact with the dynein light chain protein DYNLRB1Bas Wanschers
Department of Cell Biology, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, Nijmegen, The Netherlands
Cell Motil Cytoskeleton 65:183-96. 2008..DYNLRB is a putative modulator of the intrinsic GTPase activity of GTP-binding proteins. In vitro we were not able to reproduce this effect on Rab6 GTPase activity... - Land of the Rising Chlamy: a report of the 11th international meeting on the Cell and Molecular Biology of Chlamydomonas held in Kobe, Japan, from May 11--15, 2004Olivier Vallon
Protist 155:373-80. 2004 - Testis-specific human small heat shock protein HSPB9 is a cancer/testis antigen, and potentially interacts with the dynein subunit TCTEL1Nicole J W de Wit
Department of Pathology, University Medical Centre Nijmegen, 6500 HB Nijmegen, The Netherlands
Eur J Cell Biol 83:337-45. 2004..Additionally, immunohistochemical staining showed co-expression of HSPB9 and TCTEL1 in similar stages of spermatogenesis and in tumour cells. The possible functional significance of this interaction is discussed... - The roadblock light chain binds a novel region of the cytoplasmic Dynein intermediate chainStephen J Susalka
Department of Cell Biology, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA
J Biol Chem 277:32939-46. 2002..In addition, this roadblock-binding domain is significantly downstream from both the Tctex1- and LC8-binding sites, supporting the hypothesis that multiple light chain family members can bind to the same intermediate chain... - Cytoplasmic dynein nomenclatureK Kevin Pfister
Department of Cell Biology, University of Virginia School of Medicine, Charlottesville, VA 22908, USA
J Cell Biol 171:411-3. 2005..This nomenclature recognizes the two distinct cytoplasmic dynein complexes and has the flexibility to accommodate the discovery of new subunits and isoforms...