Protein Sorting at the <i>trans</i>-Golgi Network

Guo, Yusong; Sirkis, Daniel W.; Schekman, Randy

doi:10.1146/annurev-cellbio-100913-013012

Cited by 208 publications

(198 citation statements)

References 267 publications

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“…Export out of the ER, for example, is orchestrated by the COPII coat machinery (reviewed in Zanetti et al, 2011), whereas COPI coats are involved in intra-Golgi transport and retrograde Golgi to ER transport (reviewed in Barlowe and Miller, 2013;Popoff et al, 2011). Exit from the TGN is mediated by clathrin (to endosomes) and by unknown coats (to the plasma membrane, Guo et al, 2014). Different transport steps involve different GTPases, for example Sar1 (in mammals there are two isoforms, SAR1A and SAR1B) in the ER exit and Arf1 in ERGolgi transport and within the Golgi, as well as a distinct sets of Rab proteins and their GAPs and GEFs (reviewed in Barlowe and Miller, 2013;Pfeffer, 2013;Zanetti et al, 2011).…”

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confidence: 99%

Inhibition of cargo export at ER-exit sites and the trans-Golgi network by the secretion inhibitor FLI-06

Yonemura

Müller

et al. 2016

Journal of Cell Science

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Export out of the endoplasmic reticulum (ER) involves the Sar1 and COPII machinery acting at ER exit sites (ERES). Whether and how cargo proteins are recruited upstream of Sar1 and COPII is unclear. Two models are conceivable, a recruitment model where cargo is actively transported through a transport factor and handed over to the Sar1 and COPII machinery in ERES, and a capture model, where cargo freely diffuses into ERES where it is captured by the Sar1 and COPII machinery. Using the novel secretion inhibitor FLI-06, we show that recruitment of the cargo VSVG to ERES is an active process upstream of Sar1 and COPII. Applying FLI-06 before concentration of VSVG in ERES completely abolishes its recruitment. In contrast, applying FLI-06 after VSVG concentration in ERES does not lead to dispersal of the concentrated VSVG, arguing that it inhibits recruitment to ERES as opposed to capture in ERES. FLI-06 also inhibits export out of the trans-Golgi network (TGN), suggesting that similar mechanisms might orchestrate cargo selection and concentration at the ER and TGN. FLI-06 does not inhibit autophagosome biogenesis and the ER-peroxisomal transport route, suggesting that these rely on different mechanisms.

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Section: Introductionmentioning

confidence: 99%

Inhibition of cargo export at ER-exit sites and the trans-Golgi network by the secretion inhibitor FLI-06

Yonemura

Müller

et al. 2016

Journal of Cell Science

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“…AP complexes are composed of four adaptin subunits: two large subunits of around 100 kD, one a-type subunit (g, a, d, or «) that mediates membrane binding and one b-subunit that interacts with clathrin; one medium (m) subunit, of around 50 kD, that recognizes sorting signals in cargo proteins; and a small s-subunit of unknown function (Boehm and Bonifacino, 2001). Several clathrin adaptors have been shown to mediate basolateral polarity in epithelial cells and neurons, including AP-1A, AP-1B, and AP-4 (Gravotta et al, 2012;Bonifacino, 2014;Guo et al, 2014). The Arabidopsis genome encodes subunits of four types of putative AP complexes (AP-1 to AP-4), including five medium subunits, named mA (m2), mB1 (m1-1), mB2 (m1-2), mC (m4), and mD (m3).…”

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Sorting Motifs Involved in the Trafficking and Localization of the PIN1 Auxin Efflux Carrier

et al. 2016

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In contrast with the wealth of recent reports about the function of m-adaptins and clathrin adaptor protein (AP) complexes, there is very little information about the motifs that determine the sorting of membrane proteins within clathrin-coated vesicles in plants. Here, we investigated putative sorting signals in the large cytosolic loop of the Arabidopsis (Arabidopsis thaliana) PIN-FORMED1 (PIN1) auxin transporter, which are involved in binding m-adaptins and thus in PIN1 trafficking and localization. We found that Phe-165 and Tyr-280, Tyr-328, and Tyr-394 are involved in the binding of different m-adaptins in vitro. However, only Phe-165, which binds mA(m2)-and mD(m3)-adaptin, was found to be essential for PIN1 trafficking and localization in vivo. The PIN1:GFP-F165A mutant showed reduced endocytosis but also localized to intracellular structures containing several layers of membranes and endoplasmic reticulum (ER) markers, suggesting that they correspond to ER or ER-derived membranes. While PIN1:GFP localized normally in a mA (m2)-adaptin mutant, it accumulated in big intracellular structures containing LysoTracker in a mD (m3)-adaptin mutant, consistent with previous results obtained with mutants of other subunits of the AP-3 complex. Our data suggest that Phe-165, through the binding of mA (m2)-and mD (m3)-adaptin, is important for PIN1 endocytosis and for PIN1 trafficking along the secretory pathway, respectively.

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“…10 Several clathrin adaptors (including AP-1A, AP-1B and AP-4) have been shown to mediate basolateral polarity in epithelial cells and neurons. [11][12][13] A lot of recent reports have investigated the function of clathrin adaptor proteins in plant cells, including their possible contribution to the polar localization of PIN1 14 and PIN2. 15 However, very little is known about the signals which are recognized by m-adaptins in plants.…”

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confidence: 99%