Study of rab6, a ras‐like GTP‐binding Protein Associated with the Golgi Complex

Goud, Bruno; Yang, Chunzhi; Roa, Michèle; Martinez, Olivier; Slepnev, Vladimir I.

doi:10.1111/j.1749-6632.1994.tb26627.x

Cited by 10 publications

(8 citation statements)

References 29 publications

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“…Rab1 is localized to the cis-Golgi and is involved in ER to Golgi transport (Segev et al 1988). Rab6 is localized to the Golgi, including the trans-Golgi network, and is involved in retrograde intra-Golgi transport and transport to the ER (Goud et al 1994;Opdam et al 2000). TANGO1 (components required for transport and Golgi organization) is an integral membrane protein at ER exit sites that facilitates cargo loading into COPII vesicles for transport to the Golgi (Saito et al 2009).…”

Section: Evolution and Diversity Of The Golgimentioning

confidence: 99%

Evolution and Diversity of the Golgi

Klute¹,

Melançon²,

Dacks³

2011

Cold Spring Harbor Perspectives in Biology

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Section: Evolution and Diversity Of The Golgimentioning

confidence: 99%

Evolution and Diversity of the Golgi

Klute¹,

Melançon²,

Dacks³

2011

Cold Spring Harbor Perspectives in Biology

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“…One of the mammalian members of this family is Rab6, which by immunolocalization and functional studies has been implicated both in late intra-Golgi transport (7) and in budding from the TGN (8) (reviewed in Ref. 9).…”

mentioning

confidence: 99%

Mutation of the Rab6 Homologue of Saccharomyces cerevisiae, YPT6, Inhibits Both Early Golgi Function and Ribosome Biosynthesis

Warner

1996

Journal of Biological Chemistry

107

108

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A screen was designed to identify temperature-sensitive mutants of Saccharomyces cerevisiae, whose transcription of both ribosomal RNA and ribosomal protein genes is repressed at the nonpermissive temperature. The gene from one such mutant was cloned by complementation. The gene encodes a predicted product that is nearly 65% identical to the human GTPase, Rab6, and is likely to be identical to the yeast gene YPT6. It is essential for growth only at elevated temperatures. The mutant strain is partially defective in the maturation of the vacuolar protein carboxypeptidase Y, as well as in the secretion of invertase, which accumulates as a core-glycosylated form characteristic of the endoplasmic reticulum or the cis-Golgi, suggesting that Ypt6p is involved in an early step of the secretory pathway, earlier than that reported for the mammalian Rab6. The mutant protein, a truncation at codon 64 of 215, has a stronger phenotype than the null allele of YPT6. Four other mutants selected for defective ribosome synthesis at the nonpermissive temperature were also found to have defects in carboxypeptidase Y maturation, giving emphasis to our previous finding that a functional secretory pathway is essential for continued ribosome synthesis. Cloning of extragenic suppressors of the ts allele of YPT6 has revealed two additional proteins that influence the secretory pathway: Ssd1p, a suppressor of many mutations, and Imh1p, which bears some homology to the C-terminal portion of the cytoskeletal proteins integrin and myosin.

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“…We thus expressed GFP-Rab6A in primary astrocytes to assess the impact of αTAT1 on Rab6A-positive vesicles. GFP-Rab6A associated with the Golgi complex and cytoplasmic vesicles as described in other cell types (Goud et al, 1994). Most of Rab6A-positive vesicles appeared to move from the Golgi apparatus to the cell periphery (movie 6) and may correspond to constitutive secretion carriers (Grigoriev et al, 2007, Grigoriev et al, 2011.…”

Section: αTat1 Controls Rab6 Vesicle Fusion At Focal Adhesionsmentioning

confidence: 67%

Microtubule acetylation but not detyrosination promotes focal adhesion dynamics and cell migration

Bance

Seetharaman

Leduc

et al. 2018

Preprint

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140 w) Microtubules play a crucial role in mesenchymal migration by controlling cell polarity and the turnover of cell adhesive structures on the extracellular matrix. The polarized functions of microtubules imply that microtubules are locally regulated. Here, we investigated the regulation and role of two major tubulin post-translational modifications, acetylation and detyrosination, which have been associated with stable microtubules. Using primary astrocytes in a wound healing assay, we show that these tubulin modifications are independently regulated during cell polarization and differently affect cell migration. In contrast to microtubule detyrosination, αTAT1-mediated microtubule acetylation increases in the vicinity of focal adhesions and promotes cell migration. We further demonstrate that αTAT1 increases focal adhesion turnover by promoting Rab6positive vesicle fusion at focal adhesions. Our results highlight the specificity of microtubule post-translational modifications and bring new insight into the regulatory functions of tubulin acetylation.

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Study of rab6, a ras‐like GTP‐binding Protein Associated with the Golgi Complex

Cited by 10 publications

References 29 publications

Evolution and Diversity of the Golgi

Evolution and Diversity of the Golgi

Mutation of the Rab6 Homologue of Saccharomyces cerevisiae, YPT6, Inhibits Both Early Golgi Function and Ribosome Biosynthesis

Microtubule acetylation but not detyrosination promotes focal adhesion dynamics and cell migration

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