Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex.

Lotti, Lavinia Vittoria; Torrisi, Maria Rosaria; Pascale, Maria; Bonatti, Stefano

doi:10.1083/jcb.118.1.43

Cited by 89 publications

(62 citation statements)

References 47 publications

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“…The immunofluorescence pattern we observed with CD8-K, p23 KDEL receptor, and CD8-E19 do not exclude their presence in the IC. However, these patterns are largely different from the ones given by proteins enriched in the IC (Saraste and Svensson, 1991;Schweizer et al, 1990;Schweizer et al, 1993;Lotti et al, 1992). We have observed that newly synthesized CD8-K and CD8-E19, in contrast to CD8-S and unmodified CD8, require several hours to undergo the initial O-glycosylation events.…”

Section: Discussionmentioning

confidence: 72%

Different Fate of a Single Reporter Protein Containing KDEL or KKXX Targeting Signals Stably Expressed in Mammalian Cells

Martire

Mottola

Pascale

et al. 1996

Journal of Biological Chemistry

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In mammalian cells, resident luminal and type I transmembrane proteins of the endoplasmic reticulum usually contain KDEL and KKXX at the carboxyl terminus. These sequences induce retrieval from compartments located downstream in the secretory pathway. It has been suggested that the retrieval may occur from multiple sites, ranging from the intermediate compartment to the trans-Golgi network. To compare the retrieval of luminal and type I membrane proteins, we have used different forms of a single reporter, the human CD8 glycoprotein, stably expressed in FRT cells. Metabolic labeling and oligosaccharide analysis show that the mechanism based on the KDEL signal is leaky. With time, the KDEL-containing CD8 form reaches the trans/ trans-Golgi network compartments, where the protein is terminally glycosylated. At this stage, the retrieval mechanism stops being effective and the protein is consequently secreted. Conversely, the mechanism based on the KKXX signal guarantees that most of the KKXXcontaining CD8 form resides in the endoplasmic reticulum, little in the Golgi complex and undetectable levels at the plasma membrane. The O-glycosylation of this protein comprises for the vast majority the sole addition of peptide-bound GalNAc that occurs in an early Golgi compartment.

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Section: Discussionmentioning

confidence: 72%

Different Fate of a Single Reporter Protein Containing KDEL or KKXX Targeting Signals Stably Expressed in Mammalian Cells

Martire

Mottola

Pascale

et al. 1996

Journal of Biological Chemistry

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“…Like ERGIC-53/p58 (Lippincott-Schwartz et al, 1990;Saraste and Svensson, 1991) and other proteins present in the cis-Golgi/intermediate compartment (ERD2: Tang et al, 1993;gp74: Alcalde et al, 1994;GM130: Nakamura et al, 1995;p210: Rios et al, 1994;GS28: Subramaniam et al, 1995), p23 does not relocate to the ER after BFA treatment. In addition, p23 colocalizes with newly synthesized VSV-G, but only when VSV-G export from the intermediate compartment is blocked at 15ЊC (Saraste and Kuismanen, 1984;Schweizer et al, 1990;Lotti et al, 1992). After release of the temperature block, when forward transport resumes, small vesicles containing the G protein are typically devoid of p23.…”

Section: Subcellular Localization Of P23mentioning

confidence: 99%

“…Indeed, p23 distributes within typical tubular elements, distal to the ER and proximal to the cis side of the Golgi complex (Rambourg and Figure 12. Clermont, 1990;Schweizer et al, 1990;Lotti et al, 1992). Like ERGIC-53/p58 (Lippincott-Schwartz et al, 1990;Saraste and Svensson, 1991) and other proteins present in the cis-Golgi/intermediate compartment (ERD2: Tang et al, 1993;gp74: Alcalde et al, 1994;GM130: Nakamura et al, 1995;p210: Rios et al, 1994;GS28: Subramaniam et al, 1995), p23 does not relocate to the ER after BFA treatment.…”

Section: Subcellular Localization Of P23mentioning

confidence: 99%

“…The tsO45-G protein remains misfolded in the ER at the nonpermissive temperature of 39.5ЊC, and is properly folded and transported to the plasma membrane at 31ЊC (Bergmann et al, 1981). Like other cargo molecules, tsO45-G accumulates in the intermediate compartment at 15ЊC Lotti et al, 1992;Pepperkok et al, 1993;Griffiths et al, 1995). Vero cells were infected with VSV tsO45, and then incubated at 39.5ЊC for 2.5 h to allow synthesis and accumulation of tsO45-G in the ER.…”

Section: After Brefeldin a Or Low Temperature Treatments P23 Localizementioning

confidence: 99%

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Involvement of the transmembrane protein p23 in biosynthetic protein transport

Rojo¹,

Pepperkok²,

Emery³

et al. 1998

Biology of the Cell

115

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Abstract. Here, we report the localization and characterization of BHKp23, a member of the p24 family of transmembrane proteins, in mammalian cells. We find that p23 is a major component of tubulovesicular membranes at the cis side of the Golgi complex (estimated density: 12,500 copies/ m 2 membrane surface area, or Ϸ 30% of the total protein). Our data indicate that BHKp23-containing membranes are part of the cisGolgi network/intermediate compartment . Using the G protein of vesicular stomatitis virus as a transmembrane cargo molecule, we find that p23 membranes are an obligatory station in forward biosynthetic membrane transport, but that p23 itself is absent from transport vesicles that carry the G protein to and beyond the Golgi complex. Our data show that p23 is not present to any significant extent in coat protein (COP) I-coated vesicles generated in vitro and does not colocalize with COP I buds and vesicles. Moreover, we find that p23 cytoplasmic domain is not involved in COP I membrane recruitment. Our data demonstrate that microinjected antibodies against the cytoplasmic tail of p23 inhibit G protein transport from the cis -Golgi network/ intermediate compartment to the cell surface, suggesting that p23 function is required for the transport of transmembrane cargo molecules. These observations together with the fact that p23 is a highly abundant component in the intermediate compartment, lead us to propose that p23 contributes to membrane structure, and that this contribution is necessary for efficient segregation and transport.

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“…For this reason, we speculated that the enriched carriers described above were derived from the Golgi. As an initial test of this hypothesis, we performed a cold temperature (19.5°C) block of anterograde traffic from the Golgi, which leads to the accumulation of cargo at the late Golgi/TGN that moves out synchronously into post-Golgi carriers upon rewarming back to 37°C, as described previously (Kreis and Lodish, 1986;Lotti et al, 1992;Polishchuk et al, 2004). We asked whether the amount of APP and Mints in our enriched carrier preparation was increased shortly after release of the block.…”

Section: Overexpression Of App Increases the Amount Of App And Mint2 mentioning

confidence: 99%

Mint3/X11γ Is an ADP-Ribosylation Factor-dependent Adaptor that Regulates the Traffic of the Alzheimer's Precursor Protein from theTrans-Golgi Network

Shrivastava-Ranjan

Faúndez

Fang

et al. 2008

MBoC

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␤-Amyloid peptides (A␤) are the major component of plaques in brains of Alzheimer's patients, and are they derived from the proteolytic processing of the ␤-amyloid precursor protein (APP). The movement of APP between organelles is highly regulated, and it is tightly connected to its processing by secretases. We proposed previously that transport of APP within the cell is mediated in part through its sorting into Mint/X11-containing carriers. To test our hypothesis, we purified APP-containing vesicles from human neuroblastoma SH-SY5Y cells, and we showed that Mint2/3 are specifically enriched and that Mint3 and APP are present in the same vesicles. Increasing cellular APP levels increased the amounts of both APP and Mint3 in purified vesicles. Additional evidence supporting an obligate role for Mint3 in traffic of APP from the trans-Golgi network to the plasma membrane include the observations that depletion of Mint3 by small interference RNA (siRNA) or mutation of the Mint binding domain of APP changes the export route of APP from the basolateral to the endosomal/lysosomal sorting route. Finally, we show that increased expression of Mint3 decreased and siRNA-mediated knockdowns increased the secretion of the neurotoxic ␤-amyloid peptide, A␤ 1-40 . Together, our data implicate Mint3 activity as a critical determinant of post-Golgi APP traffic. INTRODUCTIONThe hallmark of Alzheimer's disease is the presence in brain of plaques that contain A␤ peptides, formed by the result of proteolytic processing of the ␤-amyloid precursor protein (APP). APP is a ubiquitous, single-pass transmembrane protein of unknown function that is highly expressed in brain. Processing involves the sequential actions of ␣-or ␤-plus ␥-secretases, each of which are found in multiple cellular locations (Kuentzel et al., 1993;Selkoe, 1998;Yan et al., 2001). Although processing may occur at any step, the trans-Golgi network (TGN) is the earliest site at which APP processing is thought to commence, and APP is internalized from the cell surface to endosomal compartments where ␥-secretase also acts (Selkoe et al., 1996;Greenfield et al., 1999;Lah and Levey, 2000;Bagshaw et al., 2003).The C-terminal domain of APP contains the tyrosinebased sorting motif, YENPTY, which is conserved across species and a determinant of APP traffic (Perez et al., 1999;Bonifacino and Traub, 2003;King et al., 2004). Such sorting motifs function by binding specific adaptors to facilitate their selective import into budding carriers and ensure specificity in cargo selection and coat recruitment. The highly conserved phosphotyrosine binding (PTB) domains in all three Mint proteins have been shown previously to bind directly to the YENPXY motif of APP (Borg et al., 1996(Borg et al., , 1998Zhang et al., 1997;Sastre et al., 1998;Tanahashi and Tabira, 1999;Tomita et al., 1999;Ho et al., 2002;Araki et al., 2003). Other PTB domain containing proteins have similarly been shown to bind APP, including the Fe65 (Sabo et al., 1999) family, Dab2 (Howell et al., 1999), JIP1b (King et al....

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Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex.

Cited by 89 publications

References 47 publications

Different Fate of a Single Reporter Protein Containing KDEL or KKXX Targeting Signals Stably Expressed in Mammalian Cells

Different Fate of a Single Reporter Protein Containing KDEL or KKXX Targeting Signals Stably Expressed in Mammalian Cells

Involvement of the transmembrane protein p23 in biosynthetic protein transport

Mint3/X11γ Is an ADP-Ribosylation Factor-dependent Adaptor that Regulates the Traffic of the Alzheimer's Precursor Protein from theTrans-Golgi Network

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