How the Golgi works: A cisternal progenitor model

Pfeffer, Suzanne R.

doi:10.1073/pnas.1011016107

Cited by 92 publications

(91 citation statements)

References 38 publications

(41 reference statements)

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“…The reasons why trafficking resumed from these dispersed Golgi elements as soon as microtubules regrew were unclear. It might be because of Golgi elements re-clustering and fusing because isolated Golgi elements might not be competent for trafficking (Glick and Luini, 2011;Pfeffer, 2010). We thus dispersed Golgi elements without removing microtubules and analyzed transport in these conditions.…”

Section: Blockade Of Post-golgi Transport Is Not Due To Golgi Dispersionmentioning

confidence: 99%

Microtubule-independent secretion requires functional maturation of Golgi elements

Fourrière

Divoux

Roceri

et al. 2016

Journal of Cell Science

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The Golgi complex is responsible for processing and sorting of secretory cargos. Microtubules are known to accelerate the transport of proteins from the endoplasmic reticulum (ER) to the Golgi complex and from the Golgi to the plasma membrane. However, whether postGolgi transport strictly requires microtubules is still unclear. Using the retention using selective hooks (RUSH) system to synchronize the trafficking of cargos, we show that anterograde transport of tumor necrosis factor (TNF) is strongly reduced without microtubules. We show that two populations of Golgi elements co-exist in these cells. A centrally located and giantin-positive Golgi complex that sustains trafficking, and newly formed peripheral Golgi mini-stacks that accumulate cargos in cells without microtubules. Using a genomeedited GFP-giantin cell line, we observe that the trafficking-competent Golgi population corresponds to the pre-existing population that was present before removal of microtubules. All Golgi elements support trafficking after long-term depletion of microtubules and after relocation of Golgi proteins to the ER after treatment with Brefeldin A. Our results demonstrate that functional maturation of Golgi elements is needed to ensure post-Golgi trafficking, and that microtubule-driven post-Golgi transport is not strictly required.

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Section: Blockade Of Post-golgi Transport Is Not Due To Golgi Dispersionmentioning

confidence: 99%

Microtubule-independent secretion requires functional maturation of Golgi elements

Fourrière

Divoux

Roceri

et al. 2016

Journal of Cell Science

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“…Alternatively, a Rab domain could pinch off from a cisterna to create a "megavesicle," which would then fuse with a later cisterna from the same Golgi stack. The transfers of Rab domains are presumed to operate in conjunction with COPI-mediated vesicular transport (Pfeffer 2010).…”

Section: Model 5: Stable Compartments As Cisternal Progenitorsmentioning

confidence: 99%

“…GTPases (Pfeffer 2010). This idea builds on studies indicating that in endosomes, Rab proteins can establish distinct domains within a membrane (Sonnichsen et al 2000) and can drive the biochemical transformation of a compartment by a process known as "Rab conversion" (Rink et al 2005;Nordmann et al 2010;Poteryaev et al 2010).…”

Section: Model 5: Stable Compartments As Cisternal Progenitorsmentioning

confidence: 99%

Models for Golgi Traffic: A Critical Assessment

Glick¹,

Luini²

2011

Cold Spring Harbor Perspectives in Biology

186

181

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“…It has been argued that membrane domains in organelles could undergo budding and scission, and hence control inter-organelle transport [11]. This raises the interesting possibility that the rate of domain formation could control the rate of transport.…”

Section: Introductionmentioning

confidence: 99%

Transient domain formation in membrane-bound organelles undergoing maturation

Dmitrieff¹,

Sens²

2013

Phys. Rev. E

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The membrane components of cellular organelles have been shown to segregate into domains as the result of biochemical maturation. We propose that the dynamical competition between maturation and lateral segregation of membrane components regulates domain formation. We study a twocomponent fluid membrane in which enzymatic reaction irreversibly converts one component into another, and phase separation triggers the formation of transient membrane domains. The maximum domains size is shown to depend on the maturation rate as a power-law similar to the one observed for domain growth with time in the absence of maturation, despite this time dependence not being verified in the case of irreversible maturation. This control of domain size by enzymatic activity could play a critical role in intra-organelle dynamics.

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How the Golgi works: A cisternal progenitor model

Cited by 92 publications

References 38 publications

Microtubule-independent secretion requires functional maturation of Golgi elements

Microtubule-independent secretion requires functional maturation of Golgi elements

Models for Golgi Traffic: A Critical Assessment

Transient domain formation in membrane-bound organelles undergoing maturation

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