Role of dynein–dynactin complex, kinesins, motor adaptors, and their phosphorylation in dendritogenesis

2020 ◽  
Vol 155 (1) ◽  
pp. 10-28 ◽  
Author(s):  
Aleksandra Tempes ◽  
Jan Weslawski ◽  
Agnieszka Brzozowska ◽  
Jacek Jaworski
Keyword(s):  
Dynactin Complex

scholarly journals Dynein Light Chain 1 Regulates Dynamin-mediated F-Actin Assembly during Sperm Individualization in Drosophila

2005 ◽  
Vol 16 (7) ◽  
pp. 3107-3116 ◽  
Author(s):  
Anindya Ghosh-Roy ◽  
Bela S. Desai ◽  
Krishanu Ray
Keyword(s):  
Light Chain ◽  
Cytoplasmic Dynein ◽  
Actin Dynamics ◽  
Dynein Light Chain ◽  
Actin Assembly ◽  
Cellular Functions ◽  
Directed Movement ◽  
Cellular Processes ◽  
Dynactin Complex

Toward the end of spermiogenesis, spermatid nuclei are compacted and the clonally related spermatids individualize to become mature and active sperm. Studies in Drosophila showed that caudal end-directed movement of a microfilament-rich structure, called investment cone, expels the cytoplasmic contents of individual spermatids. F-actin dynamics plays an important role in this process. Here we report that the dynein light chain 1 (DLC1) of Drosophila is involved in two separate cellular processes during sperm individualization. It is enriched around spermatid nuclei during postelongation stages and plays an important role in the dynein-dynactin–dependent rostral retention of the nuclei during this period. In addition, DDLC1 colocalizes with dynamin along investment cones and regulates F-actin assembly at this organelle by retaining dynamin along the cones. Interestingly, we found that this process does not require the other subunits of cytoplasmic dynein-dynactin complex. Altogether, these observations suggest that DLC1 could independently regulate multiple cellular functions and established a novel role of this protein in F-actin assembly in Drosophila.

scholarly journals Systematic dissection of dynein regulators in mitosis

2013 ◽  
Vol 201 (2) ◽  
pp. 201-215 ◽  
Author(s):  
Jonne A. Raaijmakers ◽  
Marvin E. Tanenbaum ◽  
René H. Medema
Keyword(s):  
Adaptor Protein ◽  
Adaptor Proteins ◽  
Cytoplasmic Dynein ◽  
Comprehensive Overview ◽  
Motor Complex ◽  
Essential Components ◽  
Complex Thought ◽  
Specific Activities ◽  
Dynactin Complex

Cytoplasmic dynein is a large minus end–directed motor complex with multiple functions during cell division. The dynein complex interacts with various adaptor proteins, including the dynactin complex, thought to be critical for most dynein functions. Specific activities have been linked to several subunits and adaptors, but the function of the majority of components has remained elusive. Here, we systematically address the function of each dynein–dynactin subunit and adaptor protein in mitosis. We identify the essential components that are required for all mitotic functions of dynein. Moreover, we find specific dynein recruitment factors, and adaptors, like Nde1/L1, required for activation, but largely dispensable for dynein localization. Most surprisingly, our data show that dynactin is not required for dynein-dependent spindle organization, but acts as a dynein recruitment factor. These results provide a comprehensive overview of the role of dynein subunits and adaptors in mitosis and reveal that dynein forms distinct complexes requiring specific recruiters and activators to promote orderly progression through mitosis.

The Role of the Dynactin Complex in Intracellular Motility

1998 ◽  
pp. 69-109 ◽  
Author(s):  
Elizabeth A. Holleran ◽  
Sher Karki ◽  
Erika L.F. Holzbaur
Keyword(s):  
Dynactin Complex ◽  
Intracellular Motility

scholarly journals LIS1 at the microtubule plus end and its role in dynein-mediated nuclear migration

2003 ◽  
Vol 160 (3) ◽  
pp. 289-290 ◽  
Author(s):  
Xin Xiang
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nuclear Migration ◽  
Cytoplasmic Dynein ◽  
Causal Gene ◽  
New Findings ◽  
Dynactin Complex

The cytoplasmic dynein complex and its accessory dynactin complex are involved in many cellular activities including nuclear migration in fungi (for review see Karki and Holzbaur, 1999). LIS1, the product of a causal gene for human lissencephaly (smooth brain), has also been implicated in dynein function based on studies in fungi and more recent studies in higher eukaryotic systems (for review see Gupta et al., 2002). Exactly how LIS1 may regulate the behavior of cytoplasmic dynein in various organisms is a fascinating question. In this issue, Lee et al. (2003) describe important new findings in Saccharomyces cerevisiae regarding the role of LIS1 (Pac1) in dynein-mediated nuclear migration.

scholarly journals A novel role of farnesylation in targeting a mitotic checkpoint protein, human Spindly, to kinetochores

2015 ◽  
Vol 208 (7) ◽  
pp. 881-896 ◽  
Author(s):  
Devinderjit K. Moudgil ◽  
Nathan Westcott ◽  
Jakub K. Famulski ◽  
Kinjal Patel ◽  
Dawn Macdonald ◽  
...  
Keyword(s):  
Mitotic Checkpoint ◽  
Cysteine Residue ◽  
Farnesyl Transferase ◽  
Checkpoint Protein ◽  
Protein Protein Interaction ◽  
Domain Mapping ◽  
Mitotic Checkpoint Protein ◽  
Dynactin Complex

Kinetochore (KT) localization of mitotic checkpoint proteins is essential for their function during mitosis. hSpindly KT localization is dependent on the RZZ complex and hSpindly recruits the dynein–dynactin complex to KTs during mitosis, but the mechanism of hSpindly KT recruitment is unknown. Through domain-mapping studies we characterized the KT localization domain of hSpindly and discovered it undergoes farnesylation at the C-terminal cysteine residue. The N-terminal 293 residues of hSpindly are dispensable for its KT localization. Inhibition of farnesylation using a farnesyl transferase inhibitor (FTI) abrogated hSpindly KT localization without affecting RZZ complex, CENP-E, and CENP-F KT localization. We showed that hSpindly is farnesylated in vivo and farnesylation is essential for its interaction with the RZZ complex and hence KT localization. FTI treatment and hSpindly knockdown displayed the same mitotic phenotypes, indicating that hSpindly is a key FTI target in mitosis. Our data show a novel role of lipidation in targeting a checkpoint protein to KTs through protein–protein interaction.

scholarly journals Evidence for a Role of CLIP-170 in the Establishment of Metaphase Chromosome Alignment

1998 ◽  
Vol 141 (4) ◽  
pp. 849-862 ◽  
Author(s):  
Denis Dujardin ◽  
U. Irene Wacker ◽  
Anne Moreau ◽  
Trina A. Schroer ◽  
Janet E. Rickard ◽  
...  
Keyword(s):  
Metaphase Plate ◽  
Polar Regions ◽  
Static Interaction ◽  
Transport Vesicles ◽  
Vitro Binding ◽  
Chromosome Alignment ◽  
Dynactin Complex

CLIPs (cytoplasmic linker proteins) are a class of proteins believed to mediate the initial, static interaction of organelles with microtubules. CLIP-170, the CLIP best characterized to date, is required for in vitro binding of endocytic transport vesicles to microtubules. We report here that CLIP-170 transiently associates with prometaphase chromosome kinetochores and codistributes with dynein and dynactin at kinetochores, but not polar regions, during mitosis. Like dynein and dynactin, a fraction of the total CLIP-170 pool can be detected on kinetochores of unattached chromosomes but not on those that have become aligned at the metaphase plate. The COOH-terminal domain of CLIP-170, when transiently overexpressed, localizes to kinetochores and causes endogenous full-length CLIP-170 to be lost from the kinetochores, resulting in a delay in prometaphase. Overexpression of the dynactin subunit, dynamitin, strongly reduces the amount of CLIP-170 at kinetochores suggesting that CLIP-170 targeting may involve the dynein/dynactin complex. Thus, CLIP-170 may be a linker for cargo in mitosis as well as interphase. However, dynein and dynactin staining at kinetochores are unaffected by this treatment and further overexpression studies indicate that neither CLIP-170 nor dynein and dynactin are required for the formation of kinetochore fibers. Nevertheless, these results strongly suggest that CLIP-170 contributes in some way to kinetochore function in vivo.

scholarly journals Molecular and Functional Basis for the Scaffolding Role of the p50/Dynamitin Subunit of the Microtubule-associated Dynactin Complex

2010 ◽  
Vol 285 (30) ◽  
pp. 23019-23031 ◽  
Author(s):  
Guillaume Jacquot ◽  
Priscilla Maidou-Peindara ◽  
Serge Benichou
Keyword(s):  
Functional Basis ◽  
Dynactin Complex

scholarly journals UNC-16/JIP3 and UNC-76/FEZ1 limit the density of mitochondria in C. elegans neurons by maintaining the balance of anterograde and retrograde mitochondrial transport

2018 ◽  
Author(s):  
Guruprasada Reddy Sure ◽  
Anusheela Chatterjee ◽  
Nikhil Mishra ◽  
Vidur Sabharwal ◽  
Swathi Devireddy ◽  
...  
Keyword(s):  
Axonal Transport ◽  
Mitochondrial Density ◽  
Neuronal Process ◽  
Kinesin Light Chain ◽  
C Elegans ◽  
Neuronal Processes ◽  
Associated Proteins ◽  
Touch Receptor Neuron ◽  
Dynactin Complex

AbstractWe investigate the role of axonal transport in regulating neuronal mitochondrial density. We show that the density of mitochondria in the touch receptor neuron (TRN) of adult Caenorhabditis elegans is constant. Mitochondrial density and transport are controlled both by the Kinesin heavy chain and the Dynein-Dynactin complex. However, unlike in other models, the presence of mitochondria in C. elegans TRNs depends on Kinesin light chain as well. Mutants in the three C. elegans miro genes do not alter mitochondrial density in the TRNs. Mutants in the Kinesin-1 associated proteins, UNC-16/JIP3 and UNC-76/FEZ1, show increased mitochondrial density and also have elevated levels of both the Kinesin Heavy and Light Chains in neurons. Genetic analyses suggest that, the increased mitochondrial density at the distal end of the neuronal process in unc-16 and unc-76 depends partly on Dynein. We observe a net anterograde bias in the ratio of anterograde to retrograde mitochondrial flux in the neuronal processes of unc-16 and unc-76, likely due to both increased Kinesin-1 and decreased Dynein in the neuronal processes. Our study shows that UNC-16 and UNC-76 indirectly limit mitochondrial density in the neuronal process maintaining a balance in anterograde and retrograde mitochondrial axonal transport.

Role of dactinomycin in the improved survival of children with Wilms' tumor

JAMA ◽  
1966 ◽  
Vol 195 (12) ◽  
pp. 1005-1009 ◽  
Author(s):  
D. J. Fernbach
Keyword(s):  
Wilms Tumor

Role of the allergist in diagnosis and management of patients with uveitis

JAMA ◽  
1966 ◽  
Vol 195 (3) ◽  
pp. 167-172 ◽  
Author(s):  
T. E. Van Metre
Keyword(s):  
Diagnosis And Management
Sign in / Sign up

Export Citation Format

Share Document