Localization of components involved in protein transport and processing through the yeast Golgi apparatus.

Franzusoff, Alex; Redding, Kevin; Crosby, J. R.; Fuller, Robert S.; Schekman, Randy

doi:10.1083/jcb.112.1.27

Cited by 249 publications

(214 citation statements)

References 42 publications

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“…Considering that Secl2p is recycling between the ER and the cis Golgi in the wild-type yeast cells and that Rerlp is involved in proper localization of Secl2p, it would be reasonable to assume the location of the Rerlp function to be either in the ER or in the Golgi. The punctate staining pattern of strongly suggests the latter possibility; a number of Golgi proteins such as Yptlp, Sec7p, and Kex2p show punctate localization in the cytoplasm (Segev et al, 1988;Franzusoff et al, 1991;Nishikawa and Nakano, 1991;Redding et al, 1991; also see below). To support this possibility, the effect of the sec7 mutation was examined.…”

Section: Rerm Encodes a Hydrophobic Proteinmentioning

confidence: 92%

Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER localization of Sec12p.

Sato

Nishikawa

Nakano

1995

MBoC

101

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Yeast Sec12p, a type II transmembrane glycoprotein, is required for formation of transport vesicles from the endoplasmic reticulum (ER). Biochemical and morphological analyses have suggested that Sec12p is localized to the ER by two mechanisms: static retention in the ER and dynamic retrieval from the early region of the Golgi apparatus. The rer1 mutant we isolated in a previous study mislocalizes the authentic Sec12p to the later compartments of the Golgi. To understand the role of RER1 on Sec12p localization, we cloned the gene and determined its reading frame. RER1 encodes a hydrophobic protein of 188 amino acid residues containing four putative membrane spanning domains. The rer1 null mutant is viable. Even in the rer1 disrupted cells, immunofluorescence of Sec12p stains the ER, implying that the retention system is still operating in the mutant. To determine the subcellular localization of Rer1p, an epitope derived from the influenza hemagglutinin was added to the C-terminus of Rer1p and the cells expressing this tagged but functional protein were observed by immunofluorescence microscopy. The anti-HA monoclonal antibody stains the cells in a punctate pattern that is typical for Golgi proteins and clearly distinct from the ER staining. This punctate staining was in fact exaggerated in the sec7 mutant that accumulates the Golgi membranes at the restrictive temperature. Furthermore, double staining of Rer1p and Ypt1p, a GTPase that is known to reside in the Golgi apparatus, showed good colocalization. Subcellular fractionation experiments indicated that the fractionation pattern of Rer1p was similar to that of an early Golgi protein, Och1p. From these results, we suggest that Rer1p functions in the Golgi membrane to return Sec12p that has escaped from the static retention system of the ER.

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Section: Rerm Encodes a Hydrophobic Proteinmentioning

confidence: 92%

Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER localization of Sec12p.

Sato

Nishikawa

Nakano

1995

MBoC

101

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“…We further analyzed the relative distribution of the cisGolgi marker Anp1p-mCherry ( Figure 1B, center panel) and the Arf GEF Sec72p-GFP ( Figure 1B, left panel), a homologue of S. cerevisiae Sec7p (Franzusoff et al, 1991) that localizes to the late Golgi compartments in budding yeast. We found that these proteins localized to several punctate structures (18 Ϯ 3 cis-and 22 Ϯ 3 trans-Golgi compartments during interphase and 23 Ϯ 3 cis-and 26 Ϯ 2 trans-Golgi compartments in dividing cells, n ϭ 10 cells).…”

Section: Organization Of the Early Secretory Pathway In S Pombementioning

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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“…of one of the Golgi compartments, in which CaZ+-mediated protein processing [5,6] and exocytosis [7,8] take place. The Ca 2+ pumping function of Pmrlp has been suggested on the basis of sequence homology to mammalian Ca z+ pumps.…”

mentioning

confidence: 99%

Elevated cytosolic free Ca²⁺ concentrations and massive Ca²⁺ accumulation within vacuoles, in yeast mutant lacking PMR1, a homolog of Ca²⁺‐ATPase

Halachmi

Eilam

1996

FEBS Letters

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Localization of components involved in protein transport and processing through the yeast Golgi apparatus.

Cited by 249 publications

References 42 publications

Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER localization of Sec12p.

Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER localization of Sec12p.

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

Elevated cytosolic free Ca²⁺ concentrations and massive Ca²⁺ accumulation within vacuoles, in yeast mutant lacking PMR1, a homolog of Ca²⁺‐ATPase

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Localization of components involved in protein transport and processing through the yeast Golgi apparatus.

Cited by 249 publications

References 42 publications

Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER localization of Sec12p.

Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER localization of Sec12p.

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

Elevated cytosolic free Ca2+ concentrations and massive Ca2+ accumulation within vacuoles, in yeast mutant lacking PMR1, a homolog of Ca2+‐ATPase

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Elevated cytosolic free Ca²⁺ concentrations and massive Ca²⁺ accumulation within vacuoles, in yeast mutant lacking PMR1, a homolog of Ca²⁺‐ATPase