IKKɛ Regulates Cell Elongation through Recycling Endosome Shuttling

Otani, Tetsuhisa; Oshima, Kenzi; Onishi, Shun; Takeda, Masaya; Shinmyozu, Kaori; Yonemura, Shigenobu; Hayashi, Shigeo

doi:10.1016/j.devcel.2011.02.001

Cited by 38 publications

(90 citation statements)

References 43 publications

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“…Interestingly, the tagged Rab11 was enriched at the distal tip of growing bristles throughout the period of bristle elongation. This was also reported by Hayashi and colleagues (Otani et al, 2011). The GFP-Rab11 at the tip was distal to the large bundles of F-actin ( Fig.…”

Section: Research Articlesupporting

confidence: 61%

Dusky-like functions as a Rab11 effector for the deposition of cuticle duringDrosophilabristle development

Nagaraj

Adler

2012

Development

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SUMMARYThe morphogenesis of Drosophila sensory bristles is dependent on the function of their actin and microtubule cytoskeleton. Actin filaments are important for bristle shape and elongation, while microtubules are thought to mediate protein and membrane trafficking to promote growth. We have identified an essential role for the bristle cuticle in the maintenance of bristle structure and shape at late stages of bristle development. We show that the small GTPase Rab11 mediates the organized deposition of chitin, a major cuticle component in bristles, and disrupting Rab11 function leads to phenotypes that result from bristle collapse rather than a failure to elongate. We further establish that Rab11 is required for the plasma membrane localization of the ZP domain-containing Dusky-like (Dyl) protein and that Dyl is also required for cuticle formation in bristles. Our data argue that Dyl functions as a Rab11 effector for mediating the attachment of the bristle cell membrane to chitin to establish a stable cuticle. Our studies also implicate the exocyst as a Rab11 effector in this process and that Rab11 trafficking along the bristle shaft is mediated by microtubules.

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Section: Research Articlesupporting

confidence: 61%

Dusky-like functions as a Rab11 effector for the deposition of cuticle duringDrosophilabristle development

Nagaraj

Adler

2012

Development

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“…Thus, when Dynein is incapable of moving cargo away from the myofiber pole, muscles are shorter than in control embryos. Indeed, a similar correlation between retrograde trafficking and directed growth was recently reported during mechanosensory bristle growth and axonal transport (Otani et al, 2011;Yi et al, 2011). Interestingly, it was recently reported that decreased retrograde transport of Dynein results in longer processes in both fibroblasts and neurons in culture (Rishal et al, 2012).…”

Section: Research Articlementioning

confidence: 75%

Muscle length and myonuclear position are independently regulated by distinct Dynein pathways

2012

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SUMMARYVarious muscle diseases present with aberrant muscle cell morphologies characterized by smaller myofibers with mispositioned nuclei. The mechanisms that normally control these processes, whether they are linked, and their contribution to muscle weakness in disease, are not known. We examined the role of Dynein and Dynein-interacting proteins during Drosophila muscle development and found that several factors, including Dynein heavy chain, Dynein light chain and Partner of inscuteable, contribute to the regulation of both muscle length and myonuclear positioning. However, Lis1 contributes only to Dynein-dependent muscle length determination, whereas CLIP-190 and Glued contribute only to Dynein-dependent myonuclear positioning. Mechanistically, microtubule density at muscle poles is decreased in CLIP-190 mutants, suggesting that microtubule-cortex interactions facilitate myonuclear positioning. In Lis1 mutants, Dynein hyperaccumulates at the muscle poles with a sharper localization pattern, suggesting that retrograde trafficking contributes to muscle length. Both Lis1 and CLIP-190 act downstream of Dynein accumulation at the cortex, suggesting that they specify Dynein function within a single location. Finally, defects in muscle length or myonuclear positioning correlate with impaired muscle function in vivo, suggesting that both processes are essential for muscle function.

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“…FIP3 directly interacts with the dynein light intermediate chain 1 of the dynein 1 motor protein complex, which directs minus-enddirected microtubule-based transport of cargo associated with FIP3 (57). Interestingly, the TBK1 and IKK⑀ kinases that phosphorylate IRF3 in the TLR4 Trif-dependent pathway are able to phosphorylate FIP3 and antagonize or redirect transport via FIP3 (58,59). This led to the hypothesis that these kinases may regulate transport of TLR4 to phagosomes via FIP3 (58).…”

Section: Discussionmentioning

confidence: 99%