scholarly journals Subunit Heterogeneity of Cytoplasmic Dynein: Differential Expression of 14 kDa Dynein Light Chains in Rat Hippocampus

2001 ◽  
Vol 21 (15) ◽  
pp. 5501-5512 ◽  
Author(s):  
Jen-Zen Chuang ◽  
Teresa A. Milner ◽  
Ching-Hwa Sung
2003 ◽  
Vol 3 ◽  
pp. 647-654 ◽  
Author(s):  
Afua Nyarko ◽  
Michael Hare ◽  
Moses Makokha ◽  
Elisar Barbar

LC8, a highly conserved 10-kDa light chain, and IC74, a 74-kDa intermediate chain, are presumed to promote the assembly of the cytoplasmic dynein motor protein complex and to be engaged in the controlled binding and release of cargo. The interactions of LC8 from Drosophila melanogaster with constructs of IC74 were characterized in vitro by affinity methods, limited proteolysis, and circular dichroism spectroscopy. Previously, we have performed limited proteolysis on the N-terminal domain of IC74, IC(1-289), when free and when bound to dynein light chains LC8 and Tctex-1[1]. We have also shown that upon addition of LC8, IC(1-289) undergoes a significant conformational change from a largely unfolded to a more ordered structure. The purpose of the work presented here is to determine whether residues 1-30 in IC74, predicted to be in a coiled coil, are involved in the stabilization of the protein upon binding to LC8. Constructs of IC74, IC(1-143), and IC(30-143) that include the LC8 binding site but with and without the first 30 residues were prepared, and their binding and protection patterns were compared to our previous results for IC(1-289). The results suggest that coiled coil residues 1-30 are not responsible for the increase in structure we observe when IC(1-289) binds to LC8.


Biochemistry ◽  
2002 ◽  
Vol 41 (13) ◽  
pp. 4302-4311 ◽  
Author(s):  
Moses Makokha ◽  
Michael Hare ◽  
Mingang Li ◽  
Thomas Hays ◽  
Elisar Barbar

2015 ◽  
Vol 208 (6) ◽  
pp. 683-692 ◽  
Author(s):  
Wenjing Li ◽  
Peishan Yi ◽  
Guangshuo Ou

Cilium formation and maintenance require intraflagellar transport (IFT). Although much is known about kinesin-2–driven anterograde IFT, the composition and regulation of retrograde IFT-specific dynein remain elusive. Components of cytoplasmic dynein may participate in IFT; however, their essential roles in cell division preclude functional studies in postmitotic cilia. Here, we report that inducible expression of the clustered regularly interspaced short palindromic repeats (CRISPR)–Cas9 system in Caenorhabditis elegans generated conditional mutations in IFT motors and particles, recapitulating ciliary defects in their null mutants. Using this method to bypass the embryonic requirement, we show the following: the dynein intermediate chain, light chain LC8, and lissencephaly-1 regulate retrograde IFT; the dynein light intermediate chain functions in dendrites and indirectly contributes to ciliogenesis; and the Tctex and Roadblock light chains are dispensable for cilium assembly. Furthermore, we demonstrate that these components undergo biphasic IFT with distinct transport frequencies and turnaround behaviors. Together, our results suggest that IFT–dynein and cytoplasmic dynein have unique compositions but also share components and regulatory mechanisms.


2004 ◽  
Vol 122 (1) ◽  
pp. 93-98 ◽  
Author(s):  
Elena Pompili ◽  
Stefania Lucia Nori ◽  
Maria Concetta Geloso ◽  
Enrico Guadagni ◽  
Valentina Corvino ◽  
...  

Author(s):  
Wen Yang ◽  
Malcolm K. Jones ◽  
Jinjiang Fan ◽  
Sheree R. Hughes-Stamm ◽  
Donald P. McManus

Biochemistry ◽  
1998 ◽  
Vol 37 (43) ◽  
pp. 15033-15041 ◽  
Author(s):  
Stephen M. King ◽  
Elisa Barbarese ◽  
James F. Dillman ◽  
Sharon E. Benashski ◽  
Khanh T. Do ◽  
...  

2007 ◽  
Vol 75 (6) ◽  
pp. 546-558 ◽  
Author(s):  
Lyubov A. Berekelya ◽  
Alexander A. Mikryukov ◽  
Natalia N. Luchinskaya ◽  
Maxim B. Ponomarev ◽  
Hugh R. Woodland ◽  
...  

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