Live imaging of yeast Golgi cisternal maturation

Matsuura-Tokita, Kumi; Takeuchi, Masaki; Ichihara, Akira; Mikuriya, Kenta; Nakano, Akihiko

doi:10.1038/nature04737

Cited by 334 publications

(334 citation statements)

References 24 publications

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“…Our data provide further evidence supporting the cisternal progression model of Golgi maturation ( Figure 1G and Supplementary Movie 3). Time required for Golgi cisternae identity change in fission yeast ( Figure 1F) was consistent with maturation dynamics reported previously in S. cerevisiae (Losev et al, 2006;Matsuura-Tokita et al, 2006). As judged by the dynamics of the early Golgi marker protein, Anp1p-mCherry, cis-Golgi cisternae could also arise de novo (Figure 1, E and F, and Supplementary Movie 2), but the relationship of these biogenesis events to tER was more difficult to establish because of the large number of Sec24p-GFP entities.…”

Section: Organization Of the Early Secretory Pathway Compartments In supporting

confidence: 90%

The Actomyosin Ring Recruits Early Secretory Compartments to the Division Site in Fission Yeast

Vještica

Tang

Oliferenko

2008

MBoC

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The ultimate goal of cytokinesis is to establish a membrane barrier between daughter cells. The fission yeast Schizosaccharomyces pombe utilizes an actomyosin-based division ring that is thought to provide physical force for the plasma membrane invagination. Ring constriction occurs concomitantly with the assembly of a division septum that is eventually cleaved. Membrane trafficking events such as targeting of secretory vesicles to the division site require a functional actomyosin ring suggesting that it serves as a spatial landmark. However, the extent of polarization of the secretion apparatus to the division site is presently unknown. We performed a survey of dynamics of several fluorophore-tagged proteins that served as markers for various compartments of the secretory pathway. These included markers for the endoplasmic reticulum, the COPII sites, and the early and late Golgi. The secretion machinery exhibited a marked polarization to the division site. Specifically, we observed an enrichment of the transitional endoplasmic reticulum (tER) accompanied by Golgi cisternae biogenesis. These processes required actomyosin ring assembly and the function of the EFC-domain protein Cdc15p. Cdc15p overexpression was sufficient to induce tER polarization in interphase. Thus, fission yeast polarizes its entire secretory machinery to the cell division site by utilizing molecular cues provided by the actomyosin ring. INTRODUCTIONCell division is the final event in the cell cycle that results in physical separation of two daughter cells. Despite being studied for more than a hundred years, the underlying molecular mechanisms and the cytological details of the process are still emerging. Various organisms and cell types have established multiple pathways to conduct cell division that are regulated at both signaling and structural levels (for review see Balasubramanian et al., 2004). In recent years, the fission yeast Schizosaccharomyces pombe has emerged as an attractive model for the study of cytokinesis because of its fully sequenced genome (Wood et al., 2002), a cell size convenient for cytological studies and the availability of a large set of conditional mutants compromised in various aspects of cell division (Chang et al., 1996;Balasubramanian et al., 1998).On entry into mitosis, S. pombe assembles an actomyosin ring that is thought to drive a binary cell fission through constriction, similar to many other eukaryotes, including nematodes, insects, and vertebrates (for review see Hales et al., 1999). During early mitosis, actin is assembled into a ring structure through the action of several actin nucleating and bundling proteins and molecular motors. These include the formin Cdc12p (Chang et al., 1997), profilin Cdc3p (Balasubramanian et al., 1992), the extended Fer/CIP4 (EFC) domain protein Cdc15p (Fankhauser et al., 1995), and the myosin heavy chain Myo2p (Kitayama et al., 1997) together with its light chains Cdc4p (McCollum et al., 1995;Naqvi et al., 1999) and Rlc1p (Le Goff et al., 2000). It has been proposed tha...

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Section: Organization Of the Early Secretory Pathway Compartments In supporting

confidence: 90%

The Actomyosin Ring Recruits Early Secretory Compartments to the Division Site in Fission Yeast

Vještica

Tang

Oliferenko

2008

MBoC

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“…Compartment maturation by Rab conversion is of special interest for the yeast Golgi complex, because live-cell video microscopy has shown that the yeast Golgi matures in a process analogous to endosome maturation in mammalian cells (9,10). Using live-cell video microscopy, Rivera-Molina and Novick (5) could also detect the conversion of a Ypt1p-enriched Golgi compartment into a Ypt32p-enriched compartment in a process that depended on the Ypt1 GAP, Gyp1p.…”

Section: Compartment Maturation By Rab Conversionmentioning

confidence: 97%

“…By using Rab GEFs and GAPs to generate late Golgi compartments from earlier Golgi compartments, yeast cells ensure vectorial and ordered transport within the secretory pathway. In rapidly growing baker's yeast cells that lack a stacked Golgi complex, Rab interconversion may provide the molecular basis for Golgi maturation in the secretory pathway (9,10). In mammalian cells in which early and late Golgi compartments seem to be more stably stacked, Rab conversion may represent part of the mechanism for vectorial transport, on top of conserved vesicle transfers between individual Golgi compartments.…”

Section: Compartment Maturation By Rab Conversionmentioning

confidence: 99%

Defining the boundaries: Rab GEFs and GAPs

Nottingham

Pfeffer

2009

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

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“…The yeast TGN appears to be a transient organelle with a half-life of only 1-2 min before it is consumed into many types of vesicles that are targeted to either the plasma membrane, early endosomes, late endosomes, the vacuole, or potentially earlier Golgi cisternae (Losev et al, 2006;Matsuura-Tokita et al, 2006). Thus, TGN residents rely on an active trafficking mechanism to maintain their TGN localization.…”

Section: Discussionmentioning

confidence: 99%

P4-ATPase Requirement for AP-1/Clathrin Function in Protein Transport from the trans-Golgi Network and Early Endosomes

Liu

Surendhran

Nothwehr

et al. 2008

MBoC

110

158

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Drs2p is a resident type 4 P-type ATPase (P4-ATPase) and potential phospholipid translocase of the trans-Golgi network (TGN) where it has been implicated in clathrin function. However, precise protein transport pathways requiring Drs2p and how it contributes to clathrin-coated vesicle budding remain unclear. Here we show a functional codependence between Drs2p and the AP-1 clathrin adaptor in protein sorting at the TGN and early endosomes of Saccharomyces cerevisiae. Genetic criteria indicate that Drs2p and AP-1 operate in the same pathway and that AP-1 requires Drs2p for function. In addition, we show that loss of AP-1 markedly increases Drs2p trafficking to the plasma membrane, but does not perturb retrieval of Drs2p from the early endosome back to the TGN. Thus AP-1 is required at the TGN to sort Drs2p out of the exocytic pathway, presumably for delivery to the early endosome. Moreover, a conditional allele that inactivates Drs2p phospholipid translocase (flippase) activity disrupts its own transport in this AP-1 pathway. Drs2p physically interacts with AP-1; however, AP-1 and clathrin are both recruited normally to the TGN in drs2⌬ cells. These results imply that Drs2p acts independently of coat recruitment to facilitate AP-1/clathrin-coated vesicle budding from the TGN. INTRODUCTIONClathrin mediates protein transport between the plasma membrane, endosomes, and TGN through association with pathway-specific adaptors that link integral membrane cargo proteins to the clathrin lattice during vesicle formation. In mammalian cells, the ubiquitously expressed heterotetrameric AP-1A clathrin adaptor, composed of ␥, ␤1, 1A, and 1-adaptins, appears to mediate both anterograde transport of proteins from the TGN to early endosomes, as well as the retrograde trip back to the TGN (Hinners and Tooze, 2003;Robinson, 2004). For its role in anterograde transport of lysosomal enzymes, AP-1A collaborates with monomeric adaptors called GGAs (Golgi localized, ␥-earcontaining, Arf-binding proteins) to recruit the mannose-6-phosphate receptor into clathrin-coated vesicles (CCVs; Doray et al., 2002). The AP-1B complex, which differs from AP-1A by an alternate 1B subunit, has a functionally distinct role in sorting cargo from the TGN to the basolateral membrane of polarized epithelial cells (Folsch et al., 1999). In budding yeast, there is evidence that AP-1 mediates early endosome to TGN retrograde transport (Valdivia et al., 2002;Foote and Nothwehr, 2006), but no anterograde role for AP-1 has yet been described. The yeast GGAs appear to function independently of AP-1 to mediate delivery of cargo from the TGN to the late endosome (Black and Pelham, 2000). Deletion of genes encoding AP-1 subunits or GGAs has little consequence to growth of yeast. However, the combined deletion of AP-1 and GGA causes a severe growth defect, suggesting that these two adaptors mediate parallel transport pathways and that yeast cannot tolerate loss of both pathways (Costaguta et al., 2001;Hirst et al., 2001).The mechanism of AP-1/clathrin-coated vesicle ...

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Live imaging of yeast Golgi cisternal maturation

Cited by 334 publications

References 24 publications

The Actomyosin Ring Recruits Early Secretory Compartments to the Division Site in Fission Yeast

The Actomyosin Ring Recruits Early Secretory Compartments to the Division Site in Fission Yeast

Defining the boundaries: Rab GEFs and GAPs

P4-ATPase Requirement for AP-1/Clathrin Function in Protein Transport from the trans-Golgi Network and Early Endosomes

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