Dhc, dynein, dynein heavy chain, cytoplasmic dynein, cytoplasmic dynein heavy chain
Gene model reviewed during 5.45
None of the polypeptides share 100% sequence identity.
Consists of at least two heavy chains and a number of intermediate and light chains.
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. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Dhc64C using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Dhc64C in GBrowse 2
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
RNAi screen using dsRNA made from templates generated with primers directed against this gene causes spindle pole detachment when assayed in S2 cells. This phenotype can be observed when the screen is performed with or without Cdc27 dsRNA.
dsRNA has been synthesised for this gene and transfected into S2 cells. S2 cells treated with this dsRNA arrest in metaphase, require 50% more time to form a metaphase plate than untreated cells and exhibit centrosome detachment and spindle focusing defects.
Dhc64C is required to maintain mRNA at its apical localization, following transport, in the blastoderm embryo.
S2 cells transfected with dsRNA made from templates generated with primers directed against this gene causes detachment of centrosomes from the spindle poles, resulting in a slight increase of spindle size.
Mitotic S2 cells treated with dsRNA made from templates generated with primers directed against this gene display a striking detachment of centrosomes from spindles and a loss of spindle pole focusing, resulting in an increase in pole-pole spacing. There is also an increase in spindle length and an elevation of the mitotic index.
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
Dhc64C may be involved in the prevention of centrosome assembly in unfertilised eggs, and establishing harmony between the chromosome and centrosome cycles.
Spindle pole movements in embryos are directed by a temporally coordinated balance of forces generated by three mitotic motors; cytoplasmic dynein, Klp61F and ncd. Dynein acts to move the poles apart throughout mitosis, and this activity is augmented by Klp61F after the fenestration of the nuclear envelope, which occurs at the onset of prometaphase. ncd generates forces that pull the poles together between interphase and metaphase, antagonising the activity of both cytoplasmic dynein and Klp61F and serving as a brake for spindle assembly.
Mutations in Dhc64C disrupt fast organelle transport in both directions in axons.
Dhc64C function is required for the attachment and migration of centrosomes along the nuclear envelope during interphase/prophase and to maintain the attachment of centrosomes to mitotic spindle poles.
Identification: PCR screen for Dynein heavy chain genes.
Mutant analysis of Dhc64C reveals cytoplasmic dynein is required at two stages of oogenesis. The localisation of dynein in mitotic cysts suggests spindle orientation is mediated by the microtubule motor cytoplasmic dynein. Later in oogenesis dynein function is necessary for proper differentiation.
Early in oogenesis mutations disrupt spindle organisation in dividing cysts and block oocyte determination.
Cytoplasmic dynein encoded by Dhc64C is essential for Drosophila viability and for cell viability in several tissues.
Clonal analysis suggests that cytoplasmic dynein mutations are cell lethal, and maternal supplies are sufficient for development to larval stages.
Cytoplasmic dynein is required for the proper formation of the oocyte early in oogenesis. Later, during oocyte growth, dynein is required for the transport of materials from the nurse cells to the developing oocyte.
Dhc64C protein acts as a minus-end directed motor that promotes microtubule translocation in vitro.
Mutation is named after a Hungarian clan that vanished by the beginning of the 14th century but their names survived in the names of settlements.
"Laborc" named for a Hungarian family that vanished by the beginning of the 14th century.