Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells

Ang, Agnes; Taguchi, Tomohiko; Francis, S.M.; Fölsch, Heike; Murrells, Lindsay J.; Pypaert, Marc; Warren, Graham; Mellman, Ira

doi:10.1083/jcb.200408165

Cited by 397 publications

(463 citation statements)

References 48 publications

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“…More importantly, using the exo70-1 mutant in the EXO70 RNAi knockdown cells, we were able to specifically examine the functional significance of Exo70-PI(4,5)P 2 interaction in VSV-G exocytosis. The exocyst has been found in various cellular compartments, including Golgi and recycling endosomes, in addition to the PM Fö lsch et al, 2003;Ang et al, 2004;Langevin et al, 2005). Here we found that the Exo70-PI(4,5)P 2 interaction is not involved in the early stages of VSV-G trafficking through the endoplasmic reticulum and Golgi.…”

Section: Discussionmentioning

confidence: 59%

“…This localization pattern contrasts that of the membrane fusion machine, the t-SNAREs, which are evenly distributed along both the mother and daughter cell membrane (Brennwald et al, 1994). In mammalian cells, the exocyst components were found in the cytosol, recycling endosomes and trans-Golgi network Fö lsch et al, 2003;Ang et al, 2004;Langevin et al, 2005). However, they are recruited to the PM during a number of cellular processes.…”

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confidence: 85%

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Phosphatidylinositol 4,5-Bisphosphate Mediates the Targeting of the Exocyst to the Plasma Membrane for Exocytosis in Mammalian Cells

Liu

Zuo

Peng

et al. 2007

MBoC

196

248

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The exocyst is an evolutionarily conserved octameric protein complex that tethers post-Golgi secretory vesicles at the plasma membrane for exocytosis. To elucidate the mechanism of vesicle tethering, it is important to understand how the exocyst physically associates with the plasma membrane (PM). In this study, we report that the mammalian exocyst subunit Exo70 associates with the PM through its direct interaction with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P 2 ). Furthermore, we have identified key conserved residues at the C-terminus of Exo70 that are crucial for the interaction of Exo70 with PI(4,5)P 2 . Disrupting Exo70-PI(4,5)P 2 interaction abolished the membrane association of Exo70. We have also found that wild-type Exo70 but not the PI(4,5)P 2 -binding-deficient Exo70 mutant is capable of recruiting other exocyst components to the PM. Using the ts045 vesicular stomatitis virus glycoprotein trafficking assay, we demonstrate that Exo70-PI(4,5)P 2 interaction is critical for the docking and fusion of post-Golgi secretory vesicles, but not for their transport to the PM. INTRODUCTIONExocytosis is important for a variety of cellular functions, ranging from the release of hormones to the incorporation of membrane proteins for cell growth and morphogenesis. The late stage of exocytosis is a multistep process that includes directional transport, tethering, docking, and fusion of postGolgi secretory vesicles with the plasma membrane (PM). The tethering step, defined as the initial contact of secretory vesicles with the PM before SNARE-mediated docking and fusion (Pfeffer, 1999;Guo et al., 2000;Waters and Hughson, 2000;Whyte and Munro, 2002), is mediated by the exocyst, an evolutionarily conserved octameric complex composed of Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70, and Exo84 (for review, see Guo et al., 2000;Hsu et al., 2004;Munson and Novick, 2006;Wang and Hsu, 2006). In budding yeast, the exocyst components localize to the growing end of the daughter cell ("bud"), where active exocytosis and membrane addition take place (TerBush and Novick, 1995;Finger et al., 1998, Guo et al., 1999. This localization pattern contrasts that of the membrane fusion machine, the t-SNAREs, which are evenly distributed along both the mother and daughter cell membrane (Brennwald et al., 1994). In mammalian cells, the exocyst components were found in the cytosol, recycling endosomes and trans-Golgi network Fö lsch et al., 2003;Ang et al., 2004;Langevin et al., 2005). However, they are recruited to the PM during a number of cellular processes. For example, in epithelial cells, the exocyst is recruited to the adherens junction region upon cell-cell contact, where it mediates protein and membrane addition at the basolateral domain (Grindstaff et al., 1998;Yeaman et al., 2001); in developing neurons, the exocyst is localized to the growing neurites, where it mediates membrane expansion (Hazuka et al., 1999;Vega and Hsu, 2001); during cell migration, the exocyst is recruited to the leading edges of the PM (Rosse et al., 2006;...

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Section: Discussionmentioning

confidence: 59%

mentioning

confidence: 85%

Phosphatidylinositol 4,5-Bisphosphate Mediates the Targeting of the Exocyst to the Plasma Membrane for Exocytosis in Mammalian Cells

Liu

Zuo

Peng

et al. 2007

MBoC

196

248

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“…The observation of an alternative pathway for APP exit from the TGN also raises the possibility that some fraction of APP is always routed via the endosomal/lysosomal route (also see Ang et al, 2004 and related studies) and that it is the abundance and relative affinities of different binding partners that determines the percentage of APP that traffics between the different alternative paths, which in turn could have an important impact on processing and A␤ generation. For example, LR11/SorLa is a lipoprotein receptor with links to Alzheimer's disease (Andersen et al, 2005;Offe et al, 2006;Rogaeva et al, 2007) that binds directly to APP in their lumenal domains (Andersen et al, 2006).…”

Section: Discussionmentioning

confidence: 95%

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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“…Similarly, Vamp8 is a component of secretory granules in secretory exocrine tissues (Wang et al, 2004;Weng et al, 2007), but is localized to a subset of endosomes in cell types that lack secretory granules (Wong et al, 1998;Antonin et al, 2000;Steegmaier et al, 2000). Both Sdmg1 and Vamp8 appear to have a function in cells lacking secretory granules (Antonin et al, 2000;Best et al, 2008), possibly related to the role of some endosomes in the secretory pathway in polarized epithelial cells (Ang et al, 2004;Lock and Stow, 2005). However, it is not clear at present what the biochemical function of Sdmg1 might be in the endosomal membrane, or whether Sdmg1 performs a similar biochemical function in secretory granule membranes.…”

Section: Discussionmentioning

confidence: 99%

Sdmg1 is a component of secretory granules in mouse secretory exocrine tissues

Best

Adams

2008

Developmental Dynamics

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Sdmg1 is a conserved eukaryotic transmembrane protein that is mainly expressed in the gonads where it may have a role in mediating signaling between somatic cells and germ cells. In this study we demonstrate that secretory exocrine cells in the pancreas, salivary gland, and mammary gland also express Sdmg1. Furthermore, we show that Sdmg1 expression is up-regulated during pancreas development when regulated secretory granules start to appear, and that Sdmg1 colocalizes with secretory granule markers in adult pancreatic acinar cells. In addition, we show that Sdmg1 co-purifies with secretory granules during subcellular fractionation of the pancreas and that Sdmg1 and the secretory granule marker Vamp2 are localized to distinct subdomains in the secretory granule membrane. These data suggest that Sdmg1 is a component of regulated secretory granules in exocrine secretory cells and that the developmental regulation of Sdmg1 expression is related to a role for Sdmg1 in post-Golgi membrane trafficking.

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Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells

Cited by 397 publications

References 48 publications

Phosphatidylinositol 4,5-Bisphosphate Mediates the Targeting of the Exocyst to the Plasma Membrane for Exocytosis in Mammalian Cells

Phosphatidylinositol 4,5-Bisphosphate Mediates the Targeting of the Exocyst to the Plasma Membrane for Exocytosis in Mammalian Cells

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

Sdmg1 is a component of secretory granules in mouse secretory exocrine tissues

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