The Identification of a Novel Endoplasmic Reticulum to Golgi SNARE Complex Used by the Prechylomicron Transport Vesicle

Siddiqi, Shadab A.; Mahan, James T.; Peggs, Kiffany; Gorelick, Fred S.; Mansbach, Charles M.

doi:10.1074/jbc.m601401200

Cited by 74 publications

(93 citation statements)

References 46 publications

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“…As to their localization, NCL, NPM1, RS10, RS18, RS3, RS3A, TBB2C, SET and SND1 had been found on ER-Golgi vesicles or Golgi membranes by proteomic analysis [31,32]. Strikingly, also FMRP, Ago2 and the Q-SNAREs Vti1a/Vti1b, which we subsequently identified as interacting proteins by immunoreactivity, reside on ER and on Golgi structures [32,[34][35][36]. The differential binding observed here for the Q-SNAREs Vti1a and Vti1b underlines C 2 -domain specificity in protein-protein interactions.…”

Section: Discussionmentioning

confidence: 99%

Synaptotagmin 11 interacts with components of the RNA‐induced silencing complex RISC in clonal pancreatic β‐cells

et al. 2014

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a b s t r a c tSynaptotagmins are two C 2 domain-containing transmembrane proteins. The function of calciumsensitive members in the regulation of post-Golgi traffic has been well established whereas little is known about the calcium-insensitive isoforms constituting half of the protein family. Novel binding partners of synaptotagmin 11 were identified in b-cells. A number of them had been assigned previously to ER/Golgi derived-vesicles or linked to RNA synthesis, translation and processing. Whereas the C2A domain interacted with the Q-SNARE Vti1a, the C2B domain of syt11 interacted with the SND1, Ago2 and FMRP, components of the RNA-induced silencing complex (RISC). Binding to SND was direct via its N-terminal tandem repeats. Our data indicate that syt11 may provide a link between gene regulation by microRNAs and membrane traffic. Structured summary of protein interactions:Syt11C2A physically interacts with Vti1a by pull down (View interaction) Syt11C2B physically interacts with SND1, PDIA6, Vti1b, Vti1a, Ago2 and FMRP by pull down (View interaction) syt11C2B binds to SND1 by filter binding (View interaction) Syt11C2B physically interacts with EIF3A, PDIA6, NPM1, EIF3B, NCL, RS3, RS3A, CBR1, ANP32B, LOC683961, SET, SND1, TBB2C, RS10 and RS18 by pull down (View interaction) SND1 physically interacts with Ago2 by anti bait coip (View interaction)

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Section: Discussionmentioning

confidence: 99%

Synaptotagmin 11 interacts with components of the RNA‐induced silencing complex RISC in clonal pancreatic β‐cells

et al. 2014

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“…One interpretation of these data is that the COPII proteins on PCTV do not un-coat prior to docking with the Golgi and thus remain during the docking process resulting in their increased concentration on isolation of the Golgi. Under conditions in which fusion with the Golgi would be expected ( 2 ), the signals for all the COPII proteins were greatly diminished ( Fig. 1A , lane 4), suggesting that the COPII proteins returned to cytosol after fusion.…”

Section: Copii Proteins Are Present At Pctv Docking With the Golgimentioning

confidence: 99%

“…To this end, we incubated PCTV, which contain all the COPII proteins ( Fig. 1A , lane 1) with Golgi under conditions that favor docking ( 2 ). Although the Golgi gave a weak signal for each of the COPII proteins prior to incubation ( Fig.…”

Section: Copii Proteins Are Present At Pctv Docking With the Golgimentioning

confidence: 99%

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Sec24C is required for docking the prechylomicron transport vesicle with the Golgi

Siddiqi

Mansbach

2010

Journal of Lipid Research

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Journal of Lipid Research Volume 51, 2010 1093anism by which dietary fat is delivered to peripheral targeted tissues, muscle, heart, and adipose tissue. The majority of the triacylglycerol (TAG) in the chylomicron is derived from hydrolytic products of dietary lipids that are resynthesized to TAG by the intestinal ER. The newly synthesized TAG crosses the ER membrane and forms the prechylomicron in the ER lumen in a two-step process ( 3 ). The exit step of the prechylomicron from the ER is the rate-limiting step by which dietary TAG traverses the intestinal absorptive cell ( 4 ) ( 5 ). Once detached from the ER membrane, the PCTV dock and then fuse with the Golgi using the N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) complex composed of VAMP7 (the R-SNARE), syntaxin5 (the Qa-SNARE), vti1A (the Qb-SNARE), and Bet1 (the Qc-SNARE) ( 2 ). Our interest in the molecular mechanism of the docking of PCTV with the Golgi in relation to the COPII proteins was raised by these fi ndings: (a) Although PCTV could be generated from ER membranes in the absence of Sar1, the initiator of the COPII complex, the vesicles formed could not fuse with the Golgi ( 1 ). The vesicles were of the same size as PCTV generated using native cytosol, contained apolipoproteinB48 (apoB48), the quintessential chylomicron apolipoprotein, and VAMP7, the R-SNARE of the PCTV-Golgi SNARE complex; however, neither docking nor fusion was possible using these vesicles. b) The liver-fatty acid binding protein (L-FABP) can, in the absence of additional cytosolic components, elaborate PCTV from intestinal ER membranes ( 6 ). However, in support of the data obtained using vesicles formed in the absence of Sar1, these L-FABP formed vesicles do not contain COPII proteins and cannot fuse with the Golgi. In Abstract The rate-limiting step in the transit of dietary fat across the intestinal absorptive cell is its exit from the endoplasmic reticulum (ER) in a specialized ER-to-Golgi transport vesicle, the prechylomicron transport vesicle (PCTV). PCTV bud off from the ER membranes and have unique features; they are the largest ER-derived vesicles (average diameter 250 nm), do not require GTP and COPII proteins for their formation, and utilize VAMP7 as a v-N-ethylmaleimide sensitive factor attachment protein receptor (SNARE). However, PCTV require COPII proteins for their fusion with the Golgi, suggesting a role for them in Golgi target recognition. In support of this, PCTV contained each of the fi ve COPII proteins when docked with the Golgi. When PCTV were fused with the Golgi, the COPII proteins were present in greatly diminished amounts, indicating they had cycled back to the cytosol. Immuno-depletion of Sec31 from the cytosol did not affect PCTV-Golgi docking, but depletion of Sec23 resulted in a 25% decrease. Immunodepletion of Sec24C caused a nearly complete cessation of PCTV docking activity, but on the addition of recombinant Sec24C, docking activity was restored. We conclude that the COPII proteins are present at docking of PCTV with...

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“…The PCTV uses VAMP7 and syntaxin 5 with rBet1 and vti1a as the cis-Golgi SNARE proteins involved in the SNARE fusion complex. The lipid composition of CMs changes in the Golgi and it is likely that they acquire apoAI in this compartment [60]. MTP is found within the Golgi apparatus and takes part in triglyceride transfer within the Golgi apparatus [61].…”

Section: Apolipoproteins and Chylomicron Synthesismentioning

confidence: 99%

Recent advances in physiological lipoprotein metabolism

Ramasamy

2014

Clinical Chemistry and Laboratory Medicine (CCLM)

184

159

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Abstract:Research into lipoprotein metabolism has developed because understanding lipoprotein metabolism has important clinical indications. Lipoproteins are risk factors for cardiovascular disease. Recent advances include the identification of factors in the synthesis and secretion of triglyceride rich lipoproteins, chylomicrons (CM) and very low density lipoproteins (VLDL). These included the identification of microsomal transfer protein, the cotranslational targeting of apoproteinB (apoB) for degradation regulated by the availability of lipids, and the characterization of transport vesicles transporting primordial apoB containing particles to the Golgi. The lipase maturation factor 1, glycosylphosphatidylinositol-anchored high density lipoprotein binding protein 1 and an angiopoietin-like protein play a role in lipoprotein lipase (LPL)-mediated hydrolysis of secreted CMs and VLDL so that the right amount of fatty acid is delivered to the right tissue at the right time. Expression of the low density lipoprotein (LDL) receptor is regulated at both transcriptional and posttranscriptional level. Proprotein convertase subtilisin/ kexin type 9 (PCSK9) has a pivotal role in the degradation of LDL receptor. Plasma remnant lipoproteins bind to specific receptors in the liver, the LDL receptor, VLDL receptor and LDL receptor-like proteins prior to removal from the plasma. Reverse cholesterol transport occurs when lipid free apoAI recruits cholesterol and phospholipid to assemble high density lipoprotein (HDL) particles. The discovery of ABC transporters (ABCA1 and ABCG1) and scavenger receptor class B type I (SR-BI) provided further information on the biogenesis of HDL. In humans HDLcholesterol can be returned to the liver either by direct uptake by SR-BI or through cholesteryl ester transfer protein exchange of cholesteryl ester for triglycerides in apoB lipoproteins, followed by hepatic uptake of apoB containing particles. Cholesterol content in cells is regulated by several transcription factors, including the liver X receptor and sterol regulatory element binding protein. This review summarizes recent advances in knowledge of the molecular mechanisms regulating lipoprotein metabolism.Keywords: ABCA1; angiopoietin-like proteins; apoC; apoAI; apolipoprotein E (apoE); cholesterol ester transfer protein; chylomicron; LDL receptor; lecithin cholesterol acyl transferase; lipoprotein(a); lipoprotein lipase; microsomal transfer protein; propertin convertase subtilisin/ kexin type 9; SR-BI; phospholipid transfer protein; very low density lipoproteins (VLDL). Abstract 1695

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The Identification of a Novel Endoplasmic Reticulum to Golgi SNARE Complex Used by the Prechylomicron Transport Vesicle

Cited by 74 publications

References 46 publications

Synaptotagmin 11 interacts with components of the RNA‐induced silencing complex RISC in clonal pancreatic β‐cells

Synaptotagmin 11 interacts with components of the RNA‐induced silencing complex RISC in clonal pancreatic β‐cells

Sec24C is required for docking the prechylomicron transport vesicle with the Golgi

Recent advances in physiological lipoprotein metabolism

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