Disease relevance of sw

• The intragenic complementation of dynein alleles reveals multiple mutant phenotypes including male and/or female sterility, bristle defects, and defects in eye development [1].
• Increased motor accumulation at microtubule plus ends may be due to increased slow plus-end movement of the bidirectional motor under hypoxia, caused by perturbation of microtubule dynamics or inactivation of the only other known Drosophila minus-end spindle motor, cytoplasmic dynein [2].
• Interactions between TcTex-1 and a diverse set of proteins such as the dynein intermediate chain, Fyn, DOC2, FIP1, the poliovirus receptor, CD155, and the rhodopsin cytoplasmic tail have been reported; yet, despite the broad range of targets, a consensus binding sequence remains uncertain [3].
• Wolbachia utilizes host microtubules and Dynein for anterior localization in the Drosophila oocyte [4].

Psychiatry related information on sw

• RESULTS: We analyzed dynein function in the oocyte by disrupting motor activity through temporally restricted expression of the dynactin subunit, dynamitin [5].
• Transport of Drosophila fragile X mental retardation protein-containing ribonucleoprotein granules by kinesin-1 and cytoplasmic dynein [6].

High impact information on sw

• Instead, apical anchoring of RNA requires microtubules and involves dynein as a static anchor that remains with the cargo at its final destination [7].
• Dynein anchors its mRNA cargo after apical transport in the Drosophila blastoderm embryo [7].
• We propose that dynein and ZYG-12 move the centrosomes toward the nucleus, followed by a ZYG-12/SUN-1-dependent anchorage [8].
• ZYG-12 is able to bind the dynein subunit DLI-1 in a two-hybrid assay and is required for dynein localization to the nuclear envelope [8].
• Homology of a 150K cytoplasmic dynein-associated polypeptide with the Drosophila gene Glued [9].

Biological context of sw

• The spatial and temporal distribution of the Glued complex during oogenesis is shown by immunocytochemistry methods to be identical to the pattern previously described for cytoplasmic dynein [10].
• A molecular genetic analysis of the interaction between the cytoplasmic dynein intermediate chain and the glued (dynactin) complex [11].
• Furthermore, our failure to recover somatic clones of cells homozygous for a Dhc64C mutation indicates that cytoplasmic dynein function is required for cell viability in several Drosophila tissues [1].
• Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein [12].
• These phenotypes are rescued by the wild-type Dic transgene, indicating that shortwing is a viable allele of the dynein intermediate chain gene and revealing a novel role for dynein function during wing development [13].

Anatomical context of sw

• The microtubule motor cytoplasmic dynein performs multiple cellular functions; however, the regulation and targeting of the motor to different cargoes is not well understood [11].
• The cytoplasmic dynein and kinesin motors have interdependent roles in patterning the Drosophila oocyte [5].
• 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 [14].
• BACKGROUND: Motor proteins of the minus end-directed cytoplasmic dynein and plus end-directed kinesin families provide the principal means for microtubule-based transport in eukaryotic cells [5].
• Cytoplasmic dynein is required for the nuclear attachment and migration of centrosomes during mitosis in Drosophila [15].

Associations of sw with chemical compounds

• Ciona outer arm dynein contains six light chains (LC) including a leucine-rich repeat protein, Tctex1- and Tctex2-related proteins, a protein similar to Drosophila roadblock and two components related to Chlamydomonas LC8 [16].
• In dynein, the first four AAA domains contain consensus nucleotide triphosphate-binding motifs, or P-loops [17].

Regulatory relationships of sw

• Dynactin is a multiprotein complex that stimulates cytoplasmic dynein-mediated vesicle motility in vitro [10].

Other interactions of sw

• Regulation of cytoplasmic dynein function in vivo by the Drosophila Glued complex [10].
• Upon addition of LC8, N-IC74 undergoes a significant conformational change from largely unfolded to a more ordered structure [18].
• The new Sdic gene is present in about 10 tandem repeats between the wildtype Cdic and AnnX genes located near the base of the X chromosome [19].
• This conformational change is reflected in increased global protection of N-IC74 from proteolytic digestion following the interaction, and in a significant change in the CD signal [18].
• Kinetochore dynein: its dynamics and role in the transport of the Rough deal checkpoint protein [20].

Analytical, diagnostic and therapeutic context of sw

• Circular dichroism, fluorescence, sedimentation velocity, and proteolysis studies indicate that N-IC74 has limited secondary and tertiary structure at near physiological solution conditions [18].
• Our findings provide a novel model system for dissection of the molecular mechanism of dynein motility [21].
• The PCR clone derived from Dhc-Yh3 is 85% identical to the corresponding region of the beta heavy chain of sea urchin flagellar dynein but only 53% identical to a cytoplasmic dynein heavy chain from Drosophila [22].
• The recent identification and sequence determination of genes encoding dynein isoforms has now permitted the in vivo analysis of dynein function in mitosis [23].
• Quantitative densitometry indicates that there is one copy of the Mr 8,000 polypeptide per IC74 [24].

References