Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex

Deshaies, Raymond J.; Sanders, Sylvia L.; Feldheim, David A.; Schekman, Randy

doi:10.1038/349806a0

Cited by 334 publications

(235 citation statements)

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“…The general ER markers such as the component of the protein translocation complex Sec63p-GFP (Deshaies et al, 1991) and the predicted oligosaccharide transferase Ost1p-GFP (Silberstein et al, 1995) exhibited both cortical and A. Vjestica et al Figure 1A), consistent with previously published work (Pidoux and Armstrong, 1993;Broughton et al, 1997). The COPII vesicle coat protein Sec24p-GFP (Barlowe et al, 1994) localized to punctate structures ( Figure 1A, left panel) of various sizes.…”

Section: Organization Of the Early Secretory Pathway In S Pombesupporting

confidence: 86%

“…The candidate proteins were selected based on their homologies to known secretory pathway markers reported in other yeast (see Materials and Methods). Tagging of these proteins did not adversely affect their essential functions judging by the normal cell morphology and division patterns.The general ER markers such as the component of the protein translocation complex Sec63p-GFP (Deshaies et al, 1991) and the predicted oligosaccharide transferase Ost1p-GFP (Silberstein et al, 1995) exhibited both cortical and A. Vjestica et al Figure 1A), consistent with previously published work (Pidoux and Armstrong, 1993;Broughton et al, 1997). The COPII vesicle coat protein Sec24p-GFP (Barlowe et al, 1994) localized to punctate structures ( Figure 1A, left panel) of various sizes.…”

supporting

confidence: 86%

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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 In S Pombesupporting

confidence: 86%

supporting

confidence: 86%

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

Vještica

Tang

Oliferenko

2008

MBoC

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“…All of the mutations result in single amino acid changes. Sec63p can form a complex with Sec6lp, Sec62p, a 23-kDa protein (p23), and a 31.5-kDa glycoprotein (gp3l.5), suggesting interactions between these proteins may be important for their function (Deshaies et al, 1991). The effect of sec62 and sec63 mutations on the cross-linking of Sec6lp to nascent chains supports this idea (Sanders et al, 1992 …”

Section: Ms176supporting

confidence: 66%

“…Genes encoding homologues of mammalian SRP or SRP receptor components have been identified (Felici et al, 1989;Hann et al, 1989Hann et al, , 1992Amaya et al, 1990;Ogg et al, 1992;Stirling and Hewitt, 1992), and depletion of these homologs causes a translocation defect in vivo (Amaya and Nakano, 1991;Hann and Walter, 1991;Ogg et al, 1992;Stirling and Hewitt, 1992). Mutations in four essential genes (SEC61, SEC62, SEC63, and KAR2) are associated with translocation defects Schekman, 1987, 1989;Toyn et al, 1988;Sadler et al, 1989;Vogel et al, 1990;, and genetic and biochemical evidence indicates physical interactions between their protein products Deshaies et al, 1991;Scidmore, Okamura, and Rose, unpublished data). Sec6lp, Sec62p, and Kar2p can be cross-linked to translocating polypeptide chains in yeast ER membranes (Musch et al, 1992;Sanders et al, 1992), suggesting that they comprise components of a common translocation apparatus.…”

Section: Introductionmentioning

confidence: 99%

Suppression of a sec63 mutation identifies a novel component of the yeast endoplasmic reticulum translocation apparatus.

Kurihara

Silver

1993

MBoC

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Mutations in the SEC63 gene are associated with defects in protein translocation into the endoplasmic reticulum (ER) as well as in nuclear protein localization in Saccharomyces cerevisiae. To identify proteins that might interact and/or function with SEC63p, we cloned a high copy suppressor (HSS1) of the temperature-sensitive lethal phenotype of the sec63-101 mutant. HSS1 is an allele-specific sec63 suppressor that encodes an integral ER membrane glycoprotein of 206 amino acids with the N-terminus in the ER lumen and C-terminal region in the cytoplasm. Haploid strains disrupted for HSS1 are temperature-sensitive for growth and accumulate precursor forms of Kar2p and invertase. The HSS1 null allele is synthetically lethal in combination with mutations affecting ER translocation. We propose that HSSlp is important for ER translocation and interacts with previously identified components of the yeast translocation apparatus. HSS1 is identical to SEC66, which encodes a glycoprotein complexed with SEC62p and SEC63p.

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“…The signal peptide (pre-peptide) of a KLK polypeptide emerging from a ribosome is bound by the signal recognition particle (SRP), which results in delayed translation and association with a membrane-bound SRP receptor (Akopian et al, 2013). Subsequently, this complex assembles with the Sec complex of the rough endoplasmic reticulum (ER) and the elongating polypeptide inserts into the Sec61 transmembrane channel (Deshaies et al, 1991;Nyathi et al, 2013). The so-called translocon complex consists of the Sec61 core and regulators, such as TRAM, TRAP, RAMP4, the oligosaccharyltransferase complex (OST), and the signal peptidase complex (SPC) (Wang and Dobberstein, 1999).…”

Section: Introductionmentioning

confidence: 99%

Sweetened kallikrein-related peptidases (KLKs): glycan trees as potential regulators of activation and activity

Guo

Skala

Magdolen

et al. 2014

Biological Chemistry

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Most kallikrein-related peptidases (KLKs) are N-glycosylated with N-acetylglucosamine 2 -mannose 9 units at Asn-Xaa-Ser/Thr sequons during protein synthesis and translocation into the endoplasmic reticulum. These N-glycans are modified in the Golgi machinery, where additional O-glycosylation at Ser and Thr takes place, before exocytotic release of the KLKs into the extracellular space. Sequons are present in all 15 members of the KLKs and comparative studies for KLKs from natural and recombinant sources elucidated some aspects of glycosylation. Although glycosylation of mammalian KLKs 1, 3, 4, 6, and 8 has been analyzed in great detail, e.g., by crystal structures, the respective function remains largely unclear. In some cases, altered enzymatic activity was observed for KLKs upon glycosylation. Remarkably, for KLK3/PSA, changes in the glycosylation pattern were observed in samples of benign prostatic hyperplasia and prostate cancer with respect to healthy individuals. Potential functions of KLK glycosylation in structural stabilization, protection against degradation, and activity modulation of substrate specificity can be deduced from a comparison with other glycosylated proteins and their regulation. According to the new concept of protein sectors, glycosylation distant from the active site might significantly influence the activity of proteases. Novel pharmacological approaches can exploit engineered glycans in the therapeutical context.

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Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex

Cited by 334 publications

References 22 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

Suppression of a sec63 mutation identifies a novel component of the yeast endoplasmic reticulum translocation apparatus.

Sweetened kallikrein-related peptidases (KLKs): glycan trees as potential regulators of activation and activity

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