A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast

Goud, Bruno; Salminen, Antti; Walworth, Nancy C.; Novick, Peter

doi:10.1016/0092-8674(88)90093-1

Cited by 579 publications

(394 citation statements)

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“…Since rab proteins, by analogy with other GTP-binding proteins, are believed to undergo a conformational change upon GTP hydrolysis and thereby to act as a molecular 'switch', it has been proposed that they mediate membrane targeting (Bourne, 1988;Bourne et al, 1990). This proposal is consistent with studies of SEC4 (Goud et al, 1988) and YPT1 in yeast (Rexach and Schekman, 1991;Oka et al, 1991;Segev, 1991). However, the precise function of rab proteins in membrane transport remains unclear.…”

Section: Introductionsupporting

confidence: 80%

“…More is known about the role of proteins of the YPT1/SEC4/rab family, which we will refer to as rab proteins. Several rab proteins have been shown to be required at specific steps of membrane transport, both in yeast (Goud et al, 1988;Segev et al, 1988) and in mammalian cells Plutner et al, 1991;Bucci et al, 1992;Lombardi et al, 1993). Moreover, every member of that family that has been localized exhibits a specific subcellular distribution (Goud and McCaffrey, 1991;Gruenberg and Clague, 1992).…”

Section: Introductionmentioning

confidence: 99%

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The N-terminal domain of a rab protein is involved in membrane-membrane recognition and/or fusion.

et al. 1994

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Proteins of the YPT1/SEC4/rab family are well documented to be involved in the regulation of membrane transport. We have previously reported that rab5 regulates endosome-endosome recognition and/or fusion in vitro. Here, we show that this process depends on the rab5 N-terminal domain. Treatment of early endosomal membranes at a low trypsin concentration essentially abolished fusion and cleaved rab5 to a 1 kDa smaller polypeptide. Two-dimensional gel analysis suggested that rab5 is one of the few, if not the only, polypeptides cleaved by trypsin under these conditions. Whereas endosome fusion could be stimulated by cytosol prepared from cells overexpressing rab5 (and thus containing high amounts of the protein), this stimulation was abolished by trypsin-treatment of the cytosol. Trypsin-treated cytosol prepared from mock-transfected cells, which contains very low amounts of rab5, showed no inhibitory activity indicating that rab5 is the target of trypsin in these experiments. Purified rab5 prepared after expression in Escherichia coli was treated with trypsin, which cleaved the protein at the N-terminus. A synthetic peptide of rab5 N-terminal domain inhibited endosome fusion in our cell-free assay. A version of the same peptide truncated at the N-terminus or a peptide of rab3 N-terminal domain were without effects. Altogether, these observations suggest that the N-terminal domain of rab5 is involved in the process of early endosome recognition and/or fusion, presumably because it interacts with another component of the transport machinery.

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Section: Introductionsupporting

confidence: 80%

Section: Introductionmentioning

confidence: 99%

The N-terminal domain of a rab protein is involved in membrane-membrane recognition and/or fusion.

et al. 1994

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“…Its surprising membrane localization suggests it has a more specialized function than thought previously and that it may regulate processes such as cross-membrane signaling or membrane trafficking. Interestingly, two other members of the CC motif-containing family, SEC4 and YPT1, associate with intracellular membranes and are thought to regulate intracellular transport of vesicles (Goud et al, 1988;Segev et al, 1988). Clearly, it will be of interest to determine the subcellular location of CK1.…”

Section: Discussionmentioning

confidence: 99%

Two genes in Saccharomyces cerevisiae encode a membrane-bound form of casein kinase-1.

Wang

Vančura

Mitcheson

et al. 1992

MBoC

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Two cDNAs encoding casein kinase-1 have been isolated from a yeast cDNA library and termed CKI1 and CKI2. Each clone encodes a protein of approximately 62,000 Da containing a highly conserved protein kinase domain surrounded by variable amino- and carboxy-terminal domains. The proteins also contain two conserved carboxy-terminal cysteine residues that comprise a consensus sequence for prenylation. Consistent with this posttranslational modification, cell fractionation experiments demonstrate that intact CKI1 is found exclusively in yeast cell membranes. Gene disruption experiments reveal that, although neither of the two CKI genes is essential by itself, at least one CKI gene is required for yeast cell viability. Spores deficient in both CKI1 and CKI2 fail to grow and, therefore, either fail to germinate or arrest as small cells before bud emergence. These results suggest that casein kinase-1, which is distributed widely in nature, plays a pivotal role in eukaryotic cell regulation.

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“…The in vivo movement and distribution of vesicles can be observed using a GFP-tagged secretory vesicle-associated rab-GTPase Sec4p (Goud et al, 1988;Mulholland et al, 1997;WalchSolimena et al, 1997;Schott et al, 2002). GFPSec4p occurs in large fluorescent masses within yeast cells, as well as discrete fluorescent particles in the mother cell.…”

Section: Yeast Lacking Bni1p or Bnr1p Exhibit Myosin-v Transport Defectsmentioning

confidence: 99%

Stable and Dynamic Axes of Polarity Use Distinct Formin Isoforms in Budding Yeast

Pruyne

Gao

et al. 2004

MBoC

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Bud growth in yeast is guided by myosin-driven delivery of secretory vesicles from the mother cell to the bud. We find transport occurs along two sets of actin cables assembled by two formin isoforms. The Bnr1p formin assembles cables that radiate from the bud neck into the mother, providing a stable mother-bud axis. These cables also depend on septins at the neck and are required for efficient transport from the mother to the bud. The Bni1p formin assembles cables that line the bud cortex and target vesicles to varying locations in the bud. Loss of these cables results in morphological defects as vesicles accumulate at the neck. Assembly of these cables depends on continued polarized secretion, suggesting vesicular transport provides a positive feedback signal for Bni1p activation, possibly by rho-proteins. By coupling different formin isoforms to unique cortical landmarks, yeast uses common cytoskeletal elements to maintain stable and dynamic axes in the same cell. INTRODUCTIONProper cell polarization requires a balance between dynamism and stability. Persistent systems, such as the apical and basolateral domains of epithelial cells, show a higher stability than flexible systems, such as cells undergoing chemotaxis. However, both types can use similar cytoskeletal components, so an important task in understanding the control of polarity is to identify features that influence persistence, and how those features integrate with the core cytoskeletal machinery providing the physical expression of polarity.The process of bud growth of the yeast Saccharomyces cerevisiae provides a model for examining the control of polarity (for reviews, see Bretscher, 2003;Chang and Peter, 2003). Secretory organelles, such as the Golgi and endoplasmic reticulum, are distributed throughout the bud and mother cell, whereas post-Golgi secretory vesicles concentrate at discrete growth sites at the cell cortex. These vesicles are guided to these sites along what are essentially two axes of polarity: a stable axis directing traffic from the mother into the bud, and a dynamic axis that fine-tunes delivery from the bud neck to specific regions in the bud, sending vesicles first to the small bud tip, then to the entire bud surface, and finally back toward the neck during mother/daughter separation. On delivery to these locations, post-Golgi vesicles fuse with the cell surface to promote localized cell expansion.Two class-V myosins, with heavy chains encoded by MYO2 (Johnston et al., 1991) and MYO4 (Haarer et al., 1994), propel cellular components, including vesicles, organelles, mRNAs, and microtubules, from the mother into the bud during growth and organelle segregation. The myosins move along cables of actin filaments that radiate throughout the cell in arrays oriented toward growth sites (Adams and Pringle, 1984;Kilmartin and Adams, 1984).Assembly of these cables depends on two formin homologues, Bni1p and Bnr1p (Evangelista et al., 2002;Sagot et al., 2002a), members of a family of cytoskeletal regulatory proteins defined by conserved fo...

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A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast

Cited by 579 publications

References 58 publications

The N-terminal domain of a rab protein is involved in membrane-membrane recognition and/or fusion.

The N-terminal domain of a rab protein is involved in membrane-membrane recognition and/or fusion.

Two genes in Saccharomyces cerevisiae encode a membrane-bound form of casein kinase-1.

Stable and Dynamic Axes of Polarity Use Distinct Formin Isoforms in Budding Yeast

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