Processing of VSVG protein is not a rate-limiting step for its efflux from the Golgi complex

Vasserman, Genady; Magal, Lee Goldstein; Shepshelovich, Jeanne; Elifaz, Eyal; Hirschberg, Koret

doi:10.1016/j.bbrc.2006.10.084

Cited by 5 publications

(5 citation statements)

References 19 publications

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“…Thus, it can be inferred that the apparent rate of VSVG-FP sorting to ERESs reported here is probably slower than the normal rate of sorting in cells with intact microtubule tracks. Nevertheless, in a quantitative analysis of ER-export dynamics carried out for the same cell type and cargo molecules, the ER-residence times for the overall ER-to-Golgi transport process were reported to be 39.4±2.3 minutes (Hirschberg and Lippincott-Schwartz, 1999) or 20.4±1.9 minutes (Vasserman et al, 2006). Thus the time constants obtained in this study for sorting are comparable to those of ER export, which relate to all of the processes, i.e.…”

Section: Journal Of Cell Sciencesupporting

confidence: 53%

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Quantitative live-cell analysis of microtubule-uncoupled cargo-protein sorting in the ER

Dukhovny

Papadopulos

Hirschberg

2008

Journal of Cell Science

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The sorting and concentration of cargo proteins within ER exit sites (ERESs) is a fundamental function of the secretory machinery. The mechanism by which peripheral coat complexes and their small GTPase effectors mediate this function with export membrane domains is only partially understood. The secretory-machinery-mediated sorting to ERESs is a process that counters the entropy-driven even distribution of membrane proteins within organellar membranes. Here, for the first time, we quantified the dynamic properties of GFP-VSVG sorting to ERESs in living cells by uncoupling it from later translocation steps using microtubule depolymerization. The dynamics of the ER to ERES redistribution of cargo proteins was quantified in single cells by measuring changes in fluorescence-intensity variance after shift to the permissive temperature. Cargo concentration within ERESs continued in cells overexpressing the GTP-locked ARF1Q71L or in the presence of brefeldin A. In the absence of COPI and microtubules, ERESs transformed from tubulovesicular to spherical membranes that actively accumulated secretory cargo and excluded ER-membrane markers. We found sorting to ERESs to be a slow and diffusion-unlimited process. Our findings exclude COPI, and identify the COPII protein complex to be directly involved in the secretory cargo sorting and redistribution functions of ERESs.

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Section: Journal Of Cell Sciencesupporting

confidence: 53%

“…VSVG-FP has been extensively used as a reporter to address dynamic properties of secretory membrane transport in living cells Presley et al, 1997;Vasserman et al, 2006). In the absence of polymerized microtubules, VSVG is sorted and concentrated in the ERES after a shift to permissive temperature.…”

Section: Introductionmentioning

confidence: 99%

Quantitative live-cell analysis of microtubule-uncoupled cargo-protein sorting in the ER

Dukhovny

Papadopulos

Hirschberg

2008

Journal of Cell Science

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“…To more formally demonstrate that VSV-G is not merely labeling a functional Golgi mini-stack after a short release, we examined its localization in C11-depleted cells after long incubation times. It has been demonstrated via live-cell imaging that VSV-G reaches the cell surface within ∼100 min after release from the ER (Hirschberg et al , 1998; Vasserman et al , 2006). Consistent with the notion that C11-depleted cells are deficient in anterograde trafficking, the VSV-G label remained punctate even 3.5 h after the shift to 32°C (Figure 6, A and B).…”

Section: Resultsmentioning

confidence: 99%

C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early stage in ER-to-Golgi trafficking

Scrivens

Noueihed

Shahrzad

et al. 2011

MBoC

110

173

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“…3p–u). VSVG, a protein known to be located at the cell membrane (Vasserman et al, 2006), was used as a control (Fig. 3v–x).…”

Section: Resultsmentioning

confidence: 99%

Conserved cellular function and stress‐mediated regulation among members of the proteolipid protein family

Fernández

Alfonso

Brocco

et al. 2009

J of Neuroscience Research

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Chronic stress causes morphological alterations in the hippocampus of rodents and tree shrews, including atrophy of CA3 dendrites and loss of synapses. The molecular mechanisms underlying these structural changes remain largely unknown. We have previously identified M6a as a stress responsive gene and shown that M6a is involved in filopodium/spine outgrowth and, likely, synapse formation. M6a belongs to the proteolipid protein (PLP) family, all of their members having four transmembrane domains that allow their localization at the plasma membrane. In the present work, we analyzed other members of this family, the closely related M6b as well as PLP and its splice variant DM20. We found that chronic restraint stress in mice reduces M6b and DM20, but not PLP, mRNA levels in the hippocampus. In addition, M6b and DM20, but again not PLP, induce filopodium formation in primary cultures of hippocampal neurons. Several M6b protein isoforms were studied, all of them having similar effects except for the one lacking the transmembrane domains. Our results reveal a conserved cellular function and a stress-mediated regulation among members of the proteolipid protein family, suggesting an involvement of proteolipid proteins in the stress response.

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Processing of VSVG protein is not a rate-limiting step for its efflux from the Golgi complex

Cited by 5 publications

References 19 publications

Quantitative live-cell analysis of microtubule-uncoupled cargo-protein sorting in the ER

Quantitative live-cell analysis of microtubule-uncoupled cargo-protein sorting in the ER

C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early stage in ER-to-Golgi trafficking

Conserved cellular function and stress‐mediated regulation among members of the proteolipid protein family

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