Persistence of Golgi Matrix Distribution Exhibits the Same Dependence on Sar1p Activity as a Golgi Glycosyltransferase

Stroud, W. J.; Shu, Jiangbo; Jack, Graham D.; Storrie, Brian

doi:10.1034/j.1600-0854.2003.00122.x

Cited by 30 publications

(52 citation statements)

References 29 publications

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“…We also found that, although the addition of recombinant protein of Sar1T39N, which is a GDP-restricted mutant of Sar1 and had been used to block COPII-dependent trafficking (Zaal et al, 1999;Ward et al, 2001;Stroud et al, 2003), inhibited anterograde transport (supplementary material Fig. S6E, Sar1T39N), it did not affect the measurements that were obtained for retrograde transport (supplementary material Fig.…”

Section: Regulation Of Rab6 Recruitment To the Golgi Membranes By Yip1amentioning

confidence: 86%

Yip1A regulates the COPI-independent retrograde transport from the Golgi complex to the ER

Kano

Yamauchi

Yoshida

et al. 2009

Journal of Cell Science

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Yip1A, a mammalian homologue of yeast Yip1p, is a multi-spanning membrane protein that is considered to be involved in transport between the endoplasmic reticulum (ER) and the Golgi. However, the precise role of Yip1A in mammalian cells remains unclear. We show here that endogenous Yip1A is localized to the ER-Golgi intermediate compartment (ERGIC). Knockdown of Yip1A by RNAi did not induce morphological changes in the Golgi, ER, or ERGIC. By analyzing a number of intracellular transport pathways, we found that Yip1A knockdown delayed the transport of Shiga toxin from the Golgi to the ER, but did not affect the anterograde transport of VSVGts045. We also found that a recombinant protein that corresponded to the N-terminal domain of Yip1A inhibited the COPI-independent retrograde transport of GFP-tagged galactosyltransferase, GT-GFP, but not the COPI-dependent retrograde transport of p58/ERGIC53. Furthermore, we found that Yip1A knockdown resulted in the dissociation of Rab6 from the membranes. These results suggested that Yip1A has a role in COPI-independent retrograde transport from the Golgi to the ER and regulates the membrane recruitment of Rab6.

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Section: Regulation Of Rab6 Recruitment To the Golgi Membranes By Yip1amentioning

confidence: 86%

Yip1A regulates the COPI-independent retrograde transport from the Golgi complex to the ER

Kano

Yamauchi

Yoshida

et al. 2009

Journal of Cell Science

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“…Storrie and colleagues (Miles et al, 2001) find that the distribution of golgins is sensitive to an ER exit block when higher concentrations of GTP-restricted Sar1p are used. Moreover, both Lippincott-Schwartz and colleagues (Ward et al, 2001) and Storrie and colleagues (Stroud et al, 2003) find that when GDP-restricted Sar1p is used to block ER exit, a condition that disrupts COPII stabilization of ER exit sites, that there is little, to no, difference in the response of Golgi matrix markers and Golgi enzymes. Both redistribute.…”

Section: Discussionmentioning

confidence: 99%

Capacity of the Golgi Apparatus for Cargo Transport Prior to Complete Assembly

Shu

Rhee

Gleeson

et al. 2006

MBoC

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In yeast, particular emphasis has been given to endoplasmic reticulum (ER)-derived, cisternal maturation models of Golgi assembly while in mammalian cells more emphasis has been given to golgins as a potentially stable assembly framework. In the case of de novo Golgi formation from the ER after brefeldin A/H89 washout in HeLa cells, we found that scattered, golgin-enriched, structures formed early and contained golgins including giantin, ranging across the entire cis to trans spectrum of the Golgi apparatus. These structures were incompetent in VSV-G cargo transport. Second, we compared Golgi competence in cargo transport to the kinetics of addition of various glycosyltransferases and glycosidases into nascent, golgin-enriched structures after drug washout. Enzyme accumulation was sequential with trans and then medial glycosyltransferases/glycosidases found in the scattered, nascent Golgi. Involvement in cargo transport preceded full accumulation of enzymes or GPP130 into nascent Golgi. Third, during mitosis, we found that the formation of a golgin-positive acceptor compartment in early telophase preceded the accumulation of a Golgi glycosyltransferase in nascent Golgi structures. We conclude that during mammalian Golgi assembly components fit into a dynamic, firstformed, multigolgin-enriched framework that is initially cargo transport incompetent. Resumption of cargo transport precedes full Golgi assembly. INTRODUCTIONDespite its key importance as the central organelle within the secretory pathway, Golgi apparatus assembly remains poorly understood (for a general review, see Shorter and Warren, 2002). The problem is complex and has been studied in several different systems. In yeast, attention has been drawn repeatedly to the relationship between the Golgi apparatus and the endoplasmic reticulum (ER). In particular, in Pichia pastoris, evidence has been presented for the de novo formation of individual Golgi apparatus membrane stacks in association with discrete ER exit sites (Bevis et al., 2002). In Saccharomyces cerevisiae, where ER exit is not organized into discrete export zones, evidence has been presented for the ER derivation of Golgi apparatus membranes in the newly formed bud (Reinke et al., 2004). The appearance of a late Golgi marker in the bud was dependent on the appearance of an early Golgi marker, consistent with the expectations of a cisternal progression/maturation model. In mammalian cells, in contrast, more emphasis has been given to the potential role of Golgi membrane clusters and Golgi matrix proteins in organizing Golgi assembly. Golgi matrix proteins belong to the golgin family of coiled-coiledrich proteins and are often, but not always, e.g., giantin, peripherally associated with Golgi apparatus membranes (for review, see Short et al., 2005). These proteins may serve a structural role in organizing Golgi apparatus membranes and subcompartments and as such may have a membrane organizing role in both mitotic and de novo mammalian Golgi assembly.In mammalian cells, the long recognized exam...

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“…The exact point of transport block differs, however, depending on the particular mutated version being expressed. Expression of a GDP-restricted form of Sar1p, designated T39N, prevents the assembly of the COPII complex and this causes disassembly of the ER exit sites (Kuge et al, 1994;Stroud et al, 2003;Ward et al, 2001). By contrast, expression of a GTP-restricted form of Sar1p, designated H79G, inhibits export from the ER exit sites which otherwise assemble normally (Miles et al, 2001;Ward et al, 2001).…”

Section: Role Of Pka Activity In Golgi Biogenesismentioning

confidence: 99%

Golgi structural stability and biogenesis depend on associated PKA activity

Bejarano

Cabrera

Vega

et al. 2006

Journal of Cell Science

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The mammalian Golgi complex consists of stacks of cisternae linked laterally into a continuous perinuclear ribbon structure. Protein kinase A is stably associated with the Golgi complex during interphase. To analyze its role in Golgi structural maintenance cells were depleted of protein kinase A regulatory subunits using small interfering RNAs. Under these conditions, the catalytic subunits redistributed to the cytosol and the entire Golgi complex underwent disassembly into multiple juxtanuclear fragments. A similar effect took place following pharmacological inhibition or redistribution of the complete holoenzyme to the cytosol. Golgi fragments maintained their polarization and competence for anterograde protein trafficking. By electron microscopy, they were identified as whorl-like structures composed of concentrically arrayed cisternae. To test a possible role of protein kinase A in Golgi biogenesis we analyzed its involvement during Golgi reassembly from the endoplasmic reticulum. In cells incubated with protein kinase A inhibitors, Golgi reconstruction was arrested at a late step of the reassembly process. This is consistent with the stage of enzyme recruitment from cytosol to emerging Golgi membranes during the reassembly process. We conclude that protein kinase A activity plays a relevant role in the assembly and maintenance of a continuous Golgi ribbon from separated membrane stacks.Supplementary material available online at

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Persistence of Golgi Matrix Distribution Exhibits the Same Dependence on Sar1p Activity as a Golgi Glycosyltransferase

Cited by 30 publications

References 29 publications

Yip1A regulates the COPI-independent retrograde transport from the Golgi complex to the ER

Yip1A regulates the COPI-independent retrograde transport from the Golgi complex to the ER

Capacity of the Golgi Apparatus for Cargo Transport Prior to Complete Assembly

Golgi structural stability and biogenesis depend on associated PKA activity

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