Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy.

Preuss, Daphne; Mulholland, Jon; Franzusoff, Alex; Segev, Nava; Botstein, David

doi:10.1091/mbc.3.7.789

Cited by 263 publications

(237 citation statements)

References 66 publications

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“…A typical Golgi element in a wild-type strain has the appearance of a curved tubular network structure, sometimes forming a complete circle (Preuss et al, 1992;Rambourg et al, 2001). In the control strain labeled with anti-HA antibodies, typical Golgi structures were observed ( Figure 5A).…”

Section: Resultsmentioning

confidence: 99%

Mutations in a Highly Conserved Region of the Arf1p ActivatorGEA2Block Anterograde Golgi Transport but Not COPI Recruitment to Membranes

Park

Hartnell

Jackson

2005

MBoC

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We have identified an important functional region of the yeast Arf1 activator Gea2p upstream of the catalytic Sec7 domain and characterized a set of temperature-sensitive (ts) mutants with amino acid substitutions in this region. These gea2-ts mutants block or slow transport of proteins traversing the secretory pathway at exit from the endoplasmic reticulum (ER) and the early Golgi, and accumulate both ER and early Golgi membranes. No defects in two types of retrograde trafficking/sorting assays were observed. We find that a substantial amount of COPI is associated with Golgi membranes in the gea2-ts mutants, even after prolonged incubation at the nonpermissive temperature. COPI in these mutants is released from Golgi membranes by brefeldin A, a drug that binds directly to Gea2p and blocks Arf1 activation. Our results demonstrate that COPI function in sorting of at least three retrograde cargo proteins within the Golgi is not perturbed in these mutants, but that forward transport is severely inhibited. Hence this region of Gea2p upstream of the Sec7 domain plays a role in anterograde transport that is independent of its role in recruiting COPI for retrograde transport, at least of a subset of Golgi-ER cargo.

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Section: Resultsmentioning

confidence: 99%

Mutations in a Highly Conserved Region of the Arf1p ActivatorGEA2Block Anterograde Golgi Transport but Not COPI Recruitment to Membranes

Park

Hartnell

Jackson

2005

MBoC

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“…The most striking difference is the physical separation of the Golgi apparatus and the ER exit sites in mammals. In yeast the distances are very small because of the small size of the cell and the fact that there are multiple dispersed Golgi throughout the cell cytoplasm (Preuss et al, 1992). Vesicles budding from the ER are never far from a Golgi.…”

Section: Discussionmentioning

confidence: 99%

An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal.

Hui

Nakamura

Sonnichsen

et al. 1997

MBoC

124

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The early Golgi t-SNARE (target-membrane-associated soluble-N-ethylmaleimide-sensitive factor attachment protein receptor) syntaxin 5 is thought to specify the docking site for both COPI and COPII coated vesicles originating from the endoplasmic reticulum (ER) and COPI vesicles on the retrograde pathway. We now show that there are two forms of syntaxin 5 that appear to be generated from the same mRNA by alternative initiation of translation. The short form (35 kDa) corresponds to the published sequence. The long form (42 kDa) has an N-terminal cytoplasmic extension containing a predicted type II ER retrieval signal. When grafted onto a reporter molecule, this signal localized the construct to the ER. Biochemical fractionation and immunofluorescence microscopy showed that there was less of the long form in the Golgi apparatus and more in peripheral punctate structures, some of which colocalized with markers of the intermediate compartment. The predicted absence of the long form in budding yeast points to a function unique to higher organisms.

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“…However, less is known about the spatial distribution of the early secretory compartments. It was reported that the Golgi apparatus also localized close to the bud site in S. cerevisiae (Preuss et al, 1992). Similarly, Bevis et al, 2002 have suggested that the Golgi elements in Pichia pastoris might preferentially localize toward the budding site.…”

Section: Introductionmentioning

confidence: 88%

“…Most published work on the involvement of protein secretion during polarity establishment has centered on targeting, localization, and delivery of post-Golgi vesicles. For example, it was shown that the early buds of the budding yeast Saccharomyces cerevisiae contain numerous secretory vesicles that are rarely observed in the mother cell (Preuss et al, 1992). Such polarized distribution depends on intact actin cables and type V myosins (Johnston et al, 1991;Govindan et al, 1995).…”

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confidence: 99%

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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Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy.

Cited by 263 publications

References 66 publications

Mutations in a Highly Conserved Region of the Arf1p ActivatorGEA2Block Anterograde Golgi Transport but Not COPI Recruitment to Membranes

Mutations in a Highly Conserved Region of the Arf1p ActivatorGEA2Block Anterograde Golgi Transport but Not COPI Recruitment to Membranes

An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal.

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

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