Dynein intermediate chain binding
WebCytoplasmic dynein and dynactin are megadalton-sized multisubunit molecules that function together as a cytoskeletal motor. In the present study, we explore the mechanism of dynein-dynactin binding in vitro and then extend our findings to an in vivo context. Solution binding assays were used to define binding domains in the dynein intermediate chain (IC) and … WebMay 15, 2024 · The remarkable ability of dynein to interact with a diverse cargo spectrum stems from its tightly regulated recruitment of cargo-specific adaptor proteins, which …
Dynein intermediate chain binding
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Web3.5.2 Dynein. Dynein is a large macromolecular complex with a molecular weight of approximately 1.2 MDa. It is composed of heavy intermediate, light intermediate, and light chains. The heavy chains contain the motor domains with six AAA ATPase domains and an MT-binding stalk ( Fig. 2.3; Oiwa and Sakakibara, 2005 ). WebFeb 12, 2015 · The dynein tail consists of two copies of the dynein heavy chain (DHC), intermediate chain (DIC2), light intermediate chain (DLIC1), and light chains (Roadblock, Tctex, and LC8). ... The requirement to form a three-way complex would reduce the chance of stochastic binding of dynein to its cargos. The shoulder coats three sides of the …
WebAlready active dynein does not need ADP-binding (Hayashi and Shingyoji, 2008). Some ODA mutants of Chlamydomonas decrease beating under viscous condition ... Dynein is … WebMar 7, 2024 · Dynein is a 1.4 MDa homodimeric complex of two heavy chains, which each binds smaller subunits, including the intermediate …
WebJun 1, 2002 · dynein intermediate chain binding Source:GO_Central. 1 publication. Molecular Function: dynein light intermediate chain binding Source:GO_Central. 1 publication. ... Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. ... WebFeb 5, 2008 · dynein light intermediate chain binding Source:GO_Central. 1 publication. Molecular Function: minus-end-directed microtubule motor activity Source:GO_Central. 1 publication. ... Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. ...
WebSep 7, 2024 · The Hook3 HBS1 region was predicted by running Colabfold 1.2.0 (no templates) on two copies of Hook3 172–287 , one copy of dynein heavy chain 576–864 …
WebMar 21, 2024 · Dynein will initiate translocation of late endosomes to microtubule minus ends only after interacting with betaIII spectrin, which requires the activities of Rab7 … ryan conlon llpWebApr 12, 2024 · Dynein is comprised of six dimeric subunits: heavy chain, intermediate chain, light-intermediate chain, and three distinct light chains. The ATPase motor is contained in the heavy chain and is comprised of six separate ATPase Associated with various cellular Activities (AAA) domains (numbered 1–6), three of which (AAA1, AAA3, … ryan connearney obituaryis doxycycline a pcnWebOct 1, 2014 · The LIC domain structure has interesting parallels with the dynein intermediate chain, which has a well-ordered WD repeat domain that interacts with the heavy chain and a less conserved disordered … ryan conlyWebJan 7, 2024 · Schroeder CM, Ostrem J, Hertz NT, Vale RD. A Ras-like domain in the light intermediate chain bridges the dynein motor to a cargo-binding region. eLife. 2014; 3:e03351. pmid:25272277 ... Mische S, He … ryan connallyWebMay 1, 2001 · The translocation of dynein along microtubules is the basis for a variety of essential cellular movements. Despite a general domain organization that is found in all the cytoskeletal motors, there are structural features of dynein that set it apart from the other motors. These include a track-binding site that is located at the tip of a long projection, … ryan connelly jdhWebFeb 6, 2024 · Previous studies have revealed that all tested cargo adaptors bind two subunits of dynein: the light-intermediate chain and the heavy chain [8. Lee I.-G. et al. ... which they designated the ‘heavy chain-binding site 1’ (HBS1) motif. Interestingly, both BICDR1 molecules in the structure use the HBS1 motif to interact with different dynein-A ... is doxycycline a sulfur drug