GTP hydrolysis by arf-1 mediates sorting and concentration of Golgi resident enzymes into functional COP I vesicles

Lanoix, Joël; Ouwendijk, Joke; Lin, Chung Chih; Stark, Annika; Love, Harold D.; Ostermann, Joachim; Nilsson, Tommy

doi:10.1093/emboj/18.18.4935

Cited by 210 publications

(214 citation statements)

References 68 publications

(107 reference statements)

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“…41,66,67 Previously, the Golgi dispersion has been explained as inhibition of vesicle formation. However, given our results that (1) ArfGAP1 overexpression leads to the accumulation of vesicles and (2) 19,20,22,23 In vitro, we found that both Arf1•GTPgS and Arf1•GTP can induce membrane deformation with cargo, coatomer, and ArfGAP1 in LUVs. However, LUVs were more extensively tubulated and deformed with Arf1•GTP than Arf1•GTPgS ( Fig.…”

Section: Discussionmentioning

confidence: 48%

“…[19][20][21][22][23] The finding that interfering with GTP hydrolysis by Arf resulted in production of transport vesicles that lacked cargo was the basis for the suggestion that GTP hydrolysis by Arf1 facilitates cargo sorting into coated vesicles. [23][24][25] The model for Arf-dependent COPI vesicle formation was modified to accommodate the result.…”

Section: Introductionmentioning

confidence: 99%

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ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

et al. 2011

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Section: Discussionmentioning

confidence: 48%

Section: Introductionmentioning

confidence: 99%

ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

et al. 2011

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“…COP I coat proteins mediate an essential and conserved retrieval pathway that continually recycles several classes of proteins, and lipids, from the cis-Golgi back to the endoplasmic reticulum (ER) Gaynor et al, 1998;Lanoix et al, 1999). Additionally, the COP I coat functions in retrograde transport and perhaps also in anterograde transport, within the Golgi complex (Orci et al, 1997;Pelham and Rothman, 2000).…”

Section: Introductionmentioning

confidence: 99%

The α- and β′-COP WD40 Domains Mediate Cargo-selective Interactions with Distinct Di-lysine Motifs

Eugster

Frigerio

Dale

et al. 2004

MBoC

102

107

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Coatomer is required for the retrieval of proteins from an early Golgi compartment back to the endoplasmic reticulum. The WD40 domain of ␣-COP is required for the recruitment of KKTN-tagged proteins into coatomer-coated vesicles. However, lack of the domain has only minor effects on growth in yeast. Here, we show that the WD40 domain of ␤ -COP is required for the recycling of the KTKLL-tagged Golgi protein Emp47p. The protein is degraded more rapidly in cells with a point mutation in the WD40 domain of ␤ -COP (sec27-95) or in cells lacking the domain altogether, whereas a point mutation in the Clathrin Heavy Chain Repeat (sec27-1) does not affect the turnover of Emp47p. Lack of the WD40 domain of ␤ -COP has only minor effects on growth of yeast cells; however, absence of both WD40 domains of ␣-and ␤ -COP is lethal. Two hybrid studies together with our analysis of the maturation of KKTN-tagged invertase and the turnover of Emp47p in ␣-and ␤ -COP mutants suggest that the two WD40 domains of ␣-and ␤ -COP bind distinct but overlapping sets of di-lysine signals and hence both contribute to recycling of proteins with di-lysine signals.

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“…This recycling helps to ensure that steady-state distributions of resident proteins are maintained within the pathway at the same time as keeping a lipid balance. Besides intra-Golgi recycling between cisternae (Hoe et al, 1995;Love et al, 1998;Lanoix et al, 1999;Lin et al, 1999), Golgi glycosylation enzymes also can recycle directly to the endoplasmic reticulum (ER). It is estimated that at least 5% of Golgi resident enzymes reside in the ER, at steady state (Pelletier et al, 2000).…”

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confidence: 99%

Regulation of Microtubule-dependent Recycling at theTrans-Golgi Network by Rab6A and Rab6A'

Young

Stauber

Nery

et al. 2005

MBoC

104

126

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The small GTPase rab6A but not the isoform rab6A has previously been identified as a regulator of the COPIindependent recycling route that carries Golgi-resident proteins and certain toxins from the Golgi to the endoplasmic reticulum (ER). The isoform rab6A has been implicated in Golgi-to-endosomal recycling. Because rab6A but not A , binds rabkinesin6, this motor protein is proposed to mediate COPI-independent recycling. We show here that both rab6A and rab6A GTP-restricted mutants promote, with similar efficiency, a microtubule-dependent recycling of Golgi resident glycosylation enzymes upon overexpression. Moreover, we used small interfering RNA mediated down-regulation of rab6A and A' expression and found that reduced levels of rab6 perturbs organization of the Golgi apparatus and delays Golgi-to-ER recycling. Rab6-directed Golgi-to-ER recycling seems to require functional dynactin, as overexpression of p50/dynamitin, or a C-terminal fragment of Bicaudal-D, both known to interact with dynactin inhibit recycling. We further present evidence that rab6-mediated recycling seems to be initiated from the trans-Golgi network. Together, this suggests that a recycling pathway operates at the level of the trans-Golgi linking directly to the ER. This pathway would be the preferred route for both toxins and resident Golgi proteins. INTRODUCTIONAnterograde flow of material through the exocytic pathway is offset by the constant recycling of both proteins and lipids. This recycling helps to ensure that steady-state distributions of resident proteins are maintained within the pathway at the same time as keeping a lipid balance. Besides intra-Golgi recycling between cisternae (Hoe et al., 1995;Love et al., 1998;Lanoix et al., 1999;Lin et al., 1999), Golgi glycosylation enzymes also can recycle directly to the endoplasmic reticulum (ER). It is estimated that at least 5% of Golgi resident enzymes reside in the ER, at steady state (Pelletier et al., 2000). This pool constitutes recycled material originating from the Golgi apparatus (Cole et al., 1998;Storrie et al., 1998).The extent of ER recycling of Golgi resident membrane proteins is sufficient to allow for complete assembly of functional Golgi stacks. Thus, upon addition of nocodazole to depolymerize microtubules, the central and juxtanuclear Golgi apparatus relocates to the 100 or so peripheral ER exit sites scattered throughout the cell. This microtubule-independent relocation occurs in the absence of any detectable elements tracking outwards from the central Golgi apparatus. Rather, the Golgi apparatus undergoes a molecular deconstruction in the trans-to-cis-direction, i.e., resident glycosylation enzymes of the trans-cisternae/trans-Golgi network (TGN) relocate with faster kinetics than do enzymes of the medial-cisternae (Yang and Storrie, 1998). Enzymes seemingly enter the ER close to the microtubule organizing center (MTOC), diffuse through the ER, and then reemerge at peripheral ER exit sites. Here, Golgi stacks are then reassembled into discrete, yet fully functiona...

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GTP hydrolysis by arf-1 mediates sorting and concentration of Golgi resident enzymes into functional COP I vesicles

Cited by 210 publications

References 68 publications

ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

The α- and β′-COP WD40 Domains Mediate Cargo-selective Interactions with Distinct Di-lysine Motifs

Regulation of Microtubule-dependent Recycling at theTrans-Golgi Network by Rab6A and Rab6A'

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