Coat/Tether Interactions—Exception or Rule?

Schröter, Saskia; Beckmann, Sabrina; Schmitt, Hans Dieter

doi:10.3389/fcell.2016.00044

Cited by 14 publications

(6 citation statements)

References 114 publications

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“…Zw10 homologs are involved in vesicle transport (43–45). Their closest homolog is Cog5, which is involved in intra-Golgi transport ( SI Appendix , Fig.…”

Section: Resultsmentioning

confidence: 99%

Mosaic origin of the eukaryotic kinetochore

Tromer

Hooff

Kops

et al. 2019

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

127

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The emergence of eukaryotes from ancient prokaryotic lineages embodied a remarkable increase in cellular complexity. While prokaryotes operate simple systems to connect DNA to the segregation machinery during cell division, eukaryotes use a highly complex protein assembly known as the kinetochore. Although conceptually similar, prokaryotic segregation systems and the eukaryotic kinetochore are not homologous. Here we investigate the origins of the kinetochore before the last eukaryotic common ancestor (LECA) using phylogenetic trees, sensitive profile-versus-profile homology detection, and structural comparisons of its protein components. We show that LECA’s kinetochore proteins share deep evolutionary histories with proteins involved in a few prokaryotic systems and a multitude of eukaryotic processes, including ubiquitination, transcription, and flagellar and vesicular transport systems. We find that gene duplications played a major role in shaping the kinetochore; more than half of LECA’s kinetochore proteins have other kinetochore proteins as closest homologs. Some of these have no detectable homology to any other eukaryotic protein, suggesting that they arose as kinetochore-specific folds before LECA. We propose that the primordial kinetochore evolved from proteins involved in various (pre)eukaryotic systems as well as evolutionarily novel folds, after which a subset duplicated to give rise to the complex kinetochore of LECA.

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“…Zw10 homologs are involved in vesicle transport (43–45). Their closest homolog is Cog5, which is involved in intra-Golgi transport ( SI Appendix , Fig.…”

Section: Resultsmentioning

confidence: 99%

Mosaic origin of the eukaryotic kinetochore

Tromer

Hooff

Kops

et al. 2019

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

127

View full text Add to dashboard Cite

show abstract

“…In addition to sorting of misfolded proteins, the vacuolar complex also serves as a site for several other important cellular activities, including biogenesis, tethering, docking and fusion of cargoes and membrane proteins for transport ( Hammer and Sellers, 2012 ; Barlowe and Miller, 2013 ). More so, the HOPS complex functions as a tether at vacuoles for different membrane and organelles including late endosomes, AP-3 transport vesicles and autophagosomes ( Schröter et al, 2016 ; Spang, 2016 ), the HOPS complex acting as tether interacts with SNAREs and/or GTPases to control the specificity of vesicle fusion in various organisms ( Janková Drdová, 2017 ).…”

Section: Introductionmentioning

confidence: 99%

A HOPS Protein, MoVps41, Is Crucially Important for Vacuolar Morphogenesis, Vegetative Growth, Reproduction and Virulence in Magnaporthe oryzae

et al. 2017

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The homotypic fusion and protein sorting protein complex (HOPS) is the first known tether complex identified in the endocytic system that plays a key role in promoting homotypic vacuolar fusion, vacuolar biogenesis and trafficking in a wide range of organisms, including plant and fungi. However, the exact influence of the HOPS complex on growth, reproduction and pathogenicity of the economically destructive rice blast fungus has not been investigated. In this study, we identified M. oryzae vacuolar protein sorting 41 (MoVps41) an accessory subunit of HOPS complex and used targeted gene deletion approach to evaluate its contribution to growth, reproduction and infectious life cycle of the rice blast fungus. Corresponding results obtained from this study showed that MoVps41 is required for optimum vegetative development of M. oryzae and observed that MoVps41 deletion mutant displayed defective vegetative growth. Our investigation further showed that MoVps41 deletion triggered vacuolar fragmentation, compromised membrane integrity and pathogenesis of the ΔMovps41 mutant. Our studies also showed for the first time that MoVps41 plays an essential role in the regulation of sexual and asexual reproduction of M. oryzae. In summary, our study provides insight into how MoVps41 mediated vacuolar fusion and biogenesis influences reproduction, pathogenesis, and vacuolar integrity in M. oryzae and also underscores the need to holistically investigate the HOPS complex in rice blast pathogen.

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“…The yeast Dsl1 multisubunit tethering complex has served as a model system for studying tether-coat interactions (10,(14)(15)(16). The Dsl1 complex is essential for retrograde Golgi-to-endoplasmic reticulum (ER) traffic mediated by COPI vesicles.…”

mentioning

confidence: 99%

Roles of singleton tryptophan motifs in COPI coat stability and vesicle tethering

Travis

Kokona

Fairman

et al. 2019

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

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Coat protein I (COPI)-coated vesicles mediate retrograde transport from the Golgi to the endoplasmic reticulum (ER), as well as transport within the Golgi. Major progress has been made in defining the structure of COPI coats, in vitro and in vivo, at resolutions as high as 9 Å. Nevertheless, important questions remain unanswered, including what specific interactions stabilize COPI coats, how COPI vesicles recognize their target membranes, and how coat disassembly is coordinated with vesicle fusion and cargo delivery. Here, we use X-ray crystallography to identify a conserved site on the COPI subunit α-COP that binds to flexible, acidic sequences containing a single tryptophan residue. One such sequence, found within α-COP itself, mediates α-COP homo-oligomerization. Another such sequence is contained within the lasso of the ER-resident Dsl1 complex, where it helps mediate the tethering of Golgi-derived COPI vesicles at the ER membrane. Together, our findings suggest that α-COP homo-oligomerization plays a key role in COPI coat stability, with potential implications for the coordination of vesicle tethering, uncoating, and fusion.

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Coat/Tether Interactions—Exception or Rule?

Cited by 14 publications

References 114 publications

Mosaic origin of the eukaryotic kinetochore

Mosaic origin of the eukaryotic kinetochore

A HOPS Protein, MoVps41, Is Crucially Important for Vacuolar Morphogenesis, Vegetative Growth, Reproduction and Virulence in Magnaporthe oryzae

Roles of singleton tryptophan motifs in COPI coat stability and vesicle tethering

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