Drosophila Ensconsin Promotes Productive Recruitment of Kinesin-1 to Microtubules

Sung, Hsin-Ho; Telley, Ivo A.; Papadaki, Piyi; Ephrussi, Anne; Surrey, Thomas; Rørth, Pernille

doi:10.1016/j.devcel.2008.10.006

Cited by 96 publications

(159 citation statements)

References 41 publications

(61 reference statements)

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“…2) and free cytoplasmic microtubules that move with the ooplasm underneath the anchored microtubules. The free cytoplasmic microtubules moved at an average of ∼460 nm·s −1 , which is consistent with kinesin-1 velocity in oocyte extracts (34)(35)(36). It should be noted that the velocities of cytoplasmic microtubules were greater than the streaming velocities observed in Fig.…”

Section: Sliding Between Cortically Anchored Microtubules and Free Cysupporting

confidence: 80%

Microtubule–microtubule sliding by kinesin-1 is essential for normal cytoplasmic streaming in Drosophila oocytes

Lü

Winding

Lakonishok

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

122

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Cytoplasmic streaming in Drosophila oocytes is a microtubulebased bulk cytoplasmic movement. Streaming efficiently circulates and localizes mRNAs and proteins deposited by the nurse cells across the oocyte. This movement is driven by kinesin-1, a major microtubule motor. Recently, we have shown that kinesin-1 heavy chain (KHC) can transport one microtubule on another microtubule, thus driving microtubule-microtubule sliding in multiple cell types. To study the role of microtubule sliding in oocyte cytoplasmic streaming, we used a Khc mutant that is deficient in microtubule sliding but able to transport a majority of cargoes. We demonstrated that streaming is reduced by genomic replacement of wild-type Khc with this sliding-deficient mutant. Streaming can be fully rescued by wild-type KHC and partially rescued by a chimeric motor that cannot move organelles but is active in microtubule sliding. Consistent with these data, we identified two populations of microtubules in fast-streaming oocytes: a network of stable microtubules anchored to the actin cortex and free cytoplasmic microtubules that moved in the ooplasm. We further demonstrated that the reduced streaming in sliding-deficient oocytes resulted in posterior determination defects. Together, we propose that kinesin-1 slides free cytoplasmic microtubules against cortically immobilized microtubules, generating forces that contribute to cytoplasmic streaming and are essential for the refinement of posterior determinants.kinesin-1 | microtubules | cytoplasmic streaming | Drosophila | axis determination

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Section: Sliding Between Cortically Anchored Microtubules and Free Cysupporting

confidence: 80%

Microtubule–microtubule sliding by kinesin-1 is essential for normal cytoplasmic streaming in Drosophila oocytes

Lü

Winding

Lakonishok

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

122

View full text Add to dashboard Cite

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“…Velocity and diffusion of a particle are then determined by fitting the mean square displacement (MSD) of a particle to the form MSD (t)v 2 t 2 +2Dt (Okada and Hirokawa, 1999). In control extracts, the average of the velocities determined for individual particles was ~340 nm/second (337±8 nm/second, n285), which is slightly lower than the velocity of purified Kinesin-1 in buffer, but similar to the speed of the motor in extracts (Blasius et al, 2007;Sung et al, 2008). In addition, we obtained mean values of 0.82±0.06 seconds for association time and 347±33 nm for run length.…”

Section: The Velocity and Run Length Of Kinesin Are Reduced In The Abmentioning

confidence: 99%

“…In vitro motility assays using purified molecules are powerful systems to obtain mechanistic insights into the function of motors, but they might eliminate physiologically relevant factors that regulate their functions (Cai et al, 2007b;Sung et al, 2008). The use of KHC-GFP ovary extracts on defined microtubule tracks allowed us to analyze active KHC with and without PAT1 under more physiological conditions.…”

Section: The Velocity and Run Length Of Kinesin Are Reduced In The Abmentioning

confidence: 99%

Drosophila PAT1 is required for Kinesin-1 to transport cargo and to maximize its motility

et al. 2010

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SUMMARYKinesin heavy chain (KHC), the force-generating component of Kinesin-1, is required for the localization of oskar mRNA and the anchoring of the nucleus in the Drosophila oocyte. These events are crucial for the establishment of the anterior-posterior and dorsal-ventral axes. KHC is also essential for the localization of Dynein and for all ooplasmic flows. Interestingly, oocytes without Kinesin light chain show no major defects in these KHC-dependent processes, suggesting that KHC binds its cargoes and is activated by a novel mechanism. Here, we shed new light on the molecular mechanism of Kinesin function in the germline. Using a combination of genetic, biochemical and motor-tracking studies, we show that PAT1, an APP-binding protein, interacts with Kinesin-1, functions in the transport of oskar mRNA and Dynein and is required for the efficient motility of KHC along microtubules. This work suggests that the role of PAT1 in cargo transport in the cell is linked to PAT1 function as a positive regulator of Kinesin motility.

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“…Defects in spermatogenesis Komada et al (2000), Sung et al (2008), Barlan et al (2013), and Metzger et al (2012) Reduced viability (in Drosophila) Myonuclear positioning altered (in Drosophila)…”

Section: Map6mentioning

confidence: 99%

“…MAP7 is a cofactor of kinesin-1 and required for organelle transport in Drosophila neurons (Barlan et al 2013). MAP7 mutants display defects in motor localization without altering MT cytoskeleton (Sung et al 2008). In addition, MAP7 has been shown to recruit kinesin-1 to the MT and regulate nuclear positioning, which is essential for skeletal muscle function in myoblasts (Metzger et al 2012).…”

Section: Map7 Family Of Microtubule-associated Proteinsmentioning

confidence: 99%

Microtubule Organization and Microtubule-Associated Proteins (MAPs)

2016

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Dendrites have a unique microtubule organization. In vertebrates, dendritic microtubules are organized in antiparallel bundles, oriented with their plus ends either pointing away or toward the soma. The mixed microtubule arrays control intracellular trafficking and local signaling pathways, and are essential for dendrite development and function. The organization of microtubule arrays largely depends on the combined function of different microtubule regulatory factors or generally named microtubule-associated proteins (MAPs). Classical MAPs, also called structural MAPs, were identified more than 20 years ago based on their ability to bind to and copurify with microtubules. Most classical MAPs bind along the microtubule lattice and regulate microtubule polymerization, bundling, and stabilization. Recent evidences suggest that classical MAPs also guide motor protein transport, interact with the actin cytoskeleton, and act in various neuronal signaling networks. Here, we give an overview of microtubule organization in dendrites and the role of classical MAPs in dendrite development, dendritic spine formation, and synaptic plasticity. IntroductionMicrotubules (MTs) are cytoskeletal structures that play essential roles in all eukaryotic cells. MTs are important not only during cell division but also in non-dividing cells, where they are critical structures in numerous cellular processes such as cell motility, migration, differentiation, intracellular transport and organelle positioning. MTs are composed of two proteins, α-and β-tubulin, that form heterodimers and organize themselves in a head-to-tail manner. MTs are dynamic and they can rapidly switch between cycles of growth and shrinkage. This MT

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Drosophila Ensconsin Promotes Productive Recruitment of Kinesin-1 to Microtubules

Cited by 96 publications

References 41 publications

Microtubule–microtubule sliding by kinesin-1 is essential for normal cytoplasmic streaming in Drosophila oocytes

Microtubule–microtubule sliding by kinesin-1 is essential for normal cytoplasmic streaming in Drosophila oocytes

Drosophila PAT1 is required for Kinesin-1 to transport cargo and to maximize its motility

Microtubule Organization and Microtubule-Associated Proteins (MAPs)

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