G protein bc subunit interaction with the dynein light-chain component Tctex-1 regulates neurite outgrowth
نویسندگان
چکیده
Pallavi Sachdev, Santosh Menon, David B Kastner, Jen-Zen Chuang, Ting-Yu Yeh, Cecilia Conde, Alfredo Caceres, Ching-Hwa Sung and Thomas P Sakmar* Laboratory of Molecular Biology and Biochemistry, The Rockefeller University, New York, NY, USA, Department of Ophthalmology, Weill Medical College of Cornell University, New York, NY, USA, INIMEC-CONICET, Cordoba, Argentina and Department of Cell and Developmental Biology, Weill Medical College of Cornell University, New York, NY, USA
منابع مشابه
The dynein light chain Tctex-1 has a dynein-independent role in actin remodeling during neurite outgrowth.
Coordinated microtubule and microfilament changes are essential for the morphological development of neurons; however, little is know about the underlying molecular machinery linking these two cytoskeletal systems. Similarly, the indispensable role of RhoGTPase family proteins has been demonstrated, but it is unknown how their activities are specifically regulated in different neurites. In this...
متن کاملEvidence for the involvement of Lfc and Tctex-1 in axon formation.
RhoA and Rac play key and opposite roles during neuronal polarization. We now show that Lfc, a guanosine nucleotide exchange factor (GEF), localizes to the Golgi apparatus and growth cones of developing neurons and negatively regulates neurite sprouting and axon formation through a Rho signaling pathway. Tctex-1, a dynein light chain implicated in axon outgrowth by modulating actin dynamics and...
متن کاملSubunit heterogeneity of cytoplasmic dynein: Differential expression of 14 kDa dynein light chains in rat hippocampus.
Cytoplasmic dynein is a multi-subunit protein complex in which each subunit is encoded by a few genes. How these subunit isoforms are assembled and regulated to mediate the diverse functions of cytoplasmic dynein is unknown. We previously have shown that two highly conserved 14 kDa dynein light chains, Tctex-1 and RP3, have different cargo-binding abilities. In this report, coimmunoprecipitatio...
متن کاملRhodopsin’s Carboxy-Terminal Cytoplasmic Tail Acts as a Membrane Receptor for Cytoplasmic Dynein by Binding to the Dynein Light Chain Tctex-1
The interaction of cytoplasmic dynein with its cargoes is thought to be indirectly mediated by dynactin, a complex that binds to the dynein intermediate chain. However, the roles of other dynein subunits in cargo binding have been unknown. Here we demonstrate that dynein translocates rhodopsin-bearing vesicles along microtubules. This interaction occurs directly between the C-terminal cytoplasm...
متن کاملThe Drosophila tctex-1 light chain is dispensable for essential cytoplasmic dynein functions but is required during spermatid differentiation.
Variations in subunit composition and modification have been proposed to regulate the multiple functions of cytoplasmic dynein. Here, we examine the role of the Drosophila ortholog of tctex-1, the 14-kDa dynein light chain. We show that the 14-kDa light chain is a bona fide component of Drosophila cytoplasmic dynein and use P element excision to generate flies that completely lack this dynein s...
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تاریخ انتشار 2013