Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning

Stuchell‐Brereton, Melissa D.; Siglin, Amanda E.; Li, Jun; Moore, Jeffrey K.; Ahmed, Shubbir; Williams, John C.; Cooper, John A.

doi:10.1091/mbc.e11-01-0075

Cited by 34 publications

(38 citation statements)

References 66 publications

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“…Similar tandem binding sites have recently been mapped in the dynein intermediate chain, Pac11, and shown to mediate Dyn2 interaction (Fig. 1, C and D) (21). To understand the molecular basis of the Dyn2-Nup159 interaction, we cloned Dyn2 from S. cerevisiae (S288c) genomic DNA into the E. coli expression vector pGEX-6P2 and expressed and purified Dyn2 to homogeneity, removing the N-terminal GST tag.…”

Section: S Cerevisiae Dyn2 Is a Member Of The Conserved Dynein Lightmentioning

confidence: 67%

“…The Dyn2-Nup159 structure creates a foundation for understanding the role of Dyn2 in the NPC as a dimerization machine that can scaffold Nup159 and extend the protein at least 170 Å (5 ϫ 34 Å). Our structural and biophysical investigations of the Dyn2-Nup159 interaction have additional implications for the Dyn2 mode of interaction and function with the dynein intermediate chain, Pac11, and for its potential role in promoting Pac11 dimerization and aiding in the recruitment of the dynein activation complex, dynactin (21).…”

Section: Discussionmentioning

confidence: 90%

“…In S. cerevisiae, Dyn2 interacts with the dynein intermediate chain, Pac11, through tandem canonical 10 -12-residue stretches, each containing a conserved QT motif (21). Similar Dyn2 binding motifs are arrayed in Nup159, where class averaged electron microscopy of the Nup159 DID region saturated with Dyn2 showed a stack of five densities like beads on a string, effectively mediating the Nup159 dimerization (11).…”

mentioning

confidence: 99%

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Structure of a Yeast Dyn2-Nup159 Complex and Molecular Basis for Dynein Light Chain-Nuclear Pore Interaction

Romes

Tripathy

Slep

2012

Journal of Biological Chemistry

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Section: S Cerevisiae Dyn2 Is a Member Of The Conserved Dynein Lightmentioning

confidence: 67%

Section: Discussionmentioning

confidence: 90%

mentioning

confidence: 99%

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Structure of a Yeast Dyn2-Nup159 Complex and Molecular Basis for Dynein Light Chain-Nuclear Pore Interaction

Romes

Tripathy

Slep

2012

Journal of Biological Chemistry

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“…Axonemal dynein promotes microtubule sliding for beating of cilia and flagella. Cytoplasmic dynein moves processively along microtubules and, in addition to organelle positioning and transport, plays key roles in cell cycle events, including nucleus-centrosome coupling, nuclear envelope breakdown, spindle assembly/positioning and chromosome segregation (Gusnowski and Srayko, 2011;Hebbar et al, 2008;Huang et al, 2011;Salina et al, 2002;Splinter et al, 2010;Stuchell-Brereton et al, 2011;Wainman et al, 2009). Dynein is a large complex composed of four subunit types: heavy (containing motor activity), light, intermediate and light intermediate chains (Höök and Vallee, 2006;Susalka and Pfister, 2000).…”

Section: Introductionmentioning

confidence: 99%

Regulation of dynein localization and centrosome positioning by Lis-1 and asunder during Drosophila spermatogenesis

et al. 2012

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Dynein, a microtubule motor complex, plays crucial roles in cell-cycle progression in many systems. The LIS1 accessory protein directly binds dynein, although its precise role in regulating dynein remains unclear. Mutation of human LIS1 causes lissencephaly, a developmental brain disorder. To gain insight into the in vivo functions of LIS1, we characterized a male-sterile allele of the Drosophila homolog of human LIS1. We found that centrosomes do not properly detach from the cell cortex at the onset of meiosis in most Lis-1 spermatocytes; centrosomes that do break cortical associations fail to attach to the nucleus. In Lis-1 spermatids, we observed loss of attachments between the nucleus, basal body and mitochondria. The localization pattern of LIS-1 protein throughout Drosophila spermatogenesis mirrors that of dynein. We show that dynein recruitment to the nuclear surface and spindle poles is severely reduced in Lis-1 male germ cells. We propose that Lis-1 spermatogenesis phenotypes are due to loss of dynein regulation, as we observed similar phenotypes in flies null for Tctex-1, a dynein light chain. We have previously identified asunder (asun) as another regulator of dynein localization and centrosome positioning during Drosophila spermatogenesis. We now report that Lis-1 is a strong dominant enhancer of asun and that localization of LIS-1 in male germ cells is ASUN dependent. We found that Drosophila LIS-1 and ASUN colocalize and coimmunoprecipitate from transfected cells, suggesting that they function within a common complex. We present a model in which Lis-1 and asun cooperate to regulate dynein localization and centrosome positioning during Drosophila spermatogenesis.

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“…The amino acid sequence VDAQTQTE (residues 99-106) of Pex17p is similar to putative Dyn2p-binding sequences found in dynein intermediate chain and Nup159p (Stelter et al, 2007;Stuchell-Brereton et al, 2011). We investigated whether V99DAQTQTE106 mediates the interaction of Pex17p with Dyn2p by constructing a series of MBP-tagged Pex17p mutants and truncations to act as potential binding partners for GSTDyn2p and GST-Pex14p in GST pull-down assays (Fig.…”

Section: Dyn2p Interacts With the Peroxisomal Matrix Protein Import Dmentioning

confidence: 99%

Dynein light chain interaction with the peroxisomal import docking complex modulates peroxisome biogenesis in yeast

Chang

Tower

Lancaster

et al. 2013

Journal of Cell Science

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SummaryDynein is a large macromolecular motor complex that moves cargo along microtubules. A motor-independent role for the light chain of dynein, Dyn2p, in peroxisome biology in Saccharomyces cerevisiae was suggested from its interaction with Pex14p, a component of the peroxisomal matrix protein import docking complex. Here we show that cells of the yeast Yarrowia lipolytica deleted for the gene encoding the homologue of Dyn2p are impaired in peroxisome function and biogenesis. These cells exhibit compromised growth on medium containing oleic acid as the carbon source, the metabolism of which requires functional peroxisomes. Their peroxisomes have abnormal morphology, atypical matrix protein localization, and an absence of proteolytic processing of the matrix enzyme thiolase, which normally occurs upon its import into the peroxisome. We also show physical and genetic interactions between Dyn2p and members of the docking complex, particularly Pex17p. Together, our results demonstrate a role for Dyn2p in the assembly of functional peroxisomes and provide evidence that Dyn2p acts in cooperation with the peroxisomal matrix protein import docking complex to effect optimal matrix protein import.

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Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning

Cited by 34 publications

References 66 publications

Structure of a Yeast Dyn2-Nup159 Complex and Molecular Basis for Dynein Light Chain-Nuclear Pore Interaction

Structure of a Yeast Dyn2-Nup159 Complex and Molecular Basis for Dynein Light Chain-Nuclear Pore Interaction

Regulation of dynein localization and centrosome positioning by Lis-1 and asunder during Drosophila spermatogenesis

Dynein light chain interaction with the peroxisomal import docking complex modulates peroxisome biogenesis in yeast

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