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Inbok Paek Lelio Orci Mariella Ravazzola Hediye Erdjument-Bromage Mylene Amherdt Paul Tempst Thomas H. S?llner James E. Rothman 《The Journal of cell biology》1997,137(5):1017-1028
We report the identification and characterization of ERS-24 (Endoplasmic Reticulum SNARE of 24 kD), a new mammalian v-SNARE implicated in vesicular transport between the ER and the Golgi. ERS24 is incorporated into 20S docking and fusion particles and disassembles from this complex in an ATP-dependent manner. ERS-24 has significant sequence homology to Sec22p, a v-SNARE in Saccharomyces cerevisiae required for transport between the ER and the Golgi. ERS-24 is localized to the ER and to the Golgi, and it is enriched in transport vesicles associated with these organelles.Newly formed transport vesicles have to be selectively targeted to their correct destinations, implying the existence of a set of compartment-specific proteins acting as unique receptor–ligand pairs. Such proteins have now been identified (Söllner et al., 1993a
; Rothman, 1994): one partner efficiently packaged into vesicles, termed a v-SNARE,1 and the other mainly localized to the target compartment, a t-SNARE. Cognate pairs of v- and t-SNAREs, capable of binding each other specifically, have been identified for the ER–Golgi transport step (Lian and Ferro-Novick, 1993; Søgaard et al., 1994), the Golgi–plasma membrane transport step (Aalto et al., 1993; Protopopov et al., 1993; Brennwald et al., 1994) in Saccharomyces cerevisiae, and regulated exocytosis in neuronal synapses (Söllner et al., 1993a
; for reviews see Scheller, 1995; Südhof, 1995). Additional components, like p115, rab proteins, and sec1 proteins, appear to regulate vesicle docking by controlling the assembly of SNARE complexes (Søgaard et al., 1994; Lian et al., 1994; Sapperstein et al., 1996; Hata et al., 1993; Pevsner et al., 1994).In contrast with vesicle docking, which requires compartment-specific components, the fusion of the two lipid bilayers uses a more general machinery derived, at least in part, from the cytosol (Rothman, 1994), which includes an ATPase, the N-ethylmaleimide–sensitive fusion protein (NSF) (Block et al., 1988; Malhotra et al., 1988), and soluble NSF attachment proteins (SNAPs) (Clary et al., 1990; Clary and Rothman, 1990; Whiteheart et al., 1993). Only the assembled v–t-SNARE complex provides high affinity sites for the consecutive binding of three SNAPs (Söllner et al., 1993b
; Hayashi et al., 1995) and NSF. When NSF is inactivated in vivo, v–t-SNARE complexes accumulate, confirming that NSF is needed for fusion after stable docking (Søgaard et al., 1994).The complex of SNAREs, SNAPs, and NSF can be isolated from detergent extracts of cellular membranes in the presence of ATPγS, or in the presence of ATP but in the absence of Mg2+, and sediments at ∼20 Svedberg (20S particle) (Wilson et al., 1992). In the presence of MgATP, the ATPase of NSF disassembles the v–t-SNARE complex and also releases SNAPs. It seems likely that this step somehow initiates fusion.To better understand vesicle flow patterns within cells, it is clearly of interest to identify new SNARE proteins. Presently, the most complete inventory is in yeast, but immunolocalization is difficult in yeast compared with animal cells, and many steps in protein transport have been reconstituted in animal extracts (Rothman, 1992) that have not yet been developed in yeast. Therefore, it is important to create an inventory of SNARE proteins in animal cells. The most unambiguous and direct method for isolating new SNAREs is to exploit their ability to assemble together with SNAPs and NSF into 20S particles and to disassemble into subunits when NSF hydrolyzes ATP. Similar approaches have already been successfully used to isolate new SNAREs implicated in ER to Golgi (Søgaard et al., 1994) and intra-Golgi transport (Nagahama et al., 1996), in addition to the original discovery of SNAREs in the context of neurotransmission (Söllner et al., 1993a
).Using this method, we now report the isolation and detailed characterization of ERS-24 (Endoplasmic Reticulum SNARE of 24 kD), a new mammalian v-SNARE that is localized to the ER and Golgi. ERS-24 is found in transport vesicles associated with the transitional areas of the ER and with the rims of Golgi cisternae, suggesting a role for ERS-24 in vesicular transport between these two compartments. 相似文献
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The changes in plant growth, relative water content (RWC), stomatal conductance, lipid peroxidation and antioxidant system in relation to the tolerance to salt stress were investigated in salt-tolerant Plantago maritima and salt-sensitive Plantago media. The 60 days old P. maritima and P. media seedlings were subjected to 0, 100 and 200 mM NaCl for 7 days. Reduction in shoot length was higher in P. media than in P. maritima after exposure to 200 mM NaCl, but 100 mM NaCl treatment did not show any effect on shoot length of P. maritima. Shoot dry weight decreased in P. media and did not change in P. maritima. Two hundred millimolar NaCl treatment had no effect on leaf RWC in P. maritima, but it was reduced in P. media. Salt stress caused reduction in stomatal conductance being more pronounced in P. media than in P. maritima. Activities of superoxide dismutase (SOD; EC 1.15.1.1), catalase (CAT; EC 1.11.1.6), glutathione reductase (GR; EC 1.6.4.2) decreased in P. media with increasing salinity. Ascorbate peroxidase (APX; EC 1.11.1.11) activity in leaves of P. media was increased and showed no change under 100 and 200 mM NaCl, respectively. However, activities of CAT, APX and GR increased under 200 mM NaCl while their activities did not change under 100 mM NaCl in P. maritima. SOD activity in leaves of P. maritima increased with increasing salinity. Concomitant with this, four SOD activity bands were identified in leaves of P. maritima, two bands only were observed in P. media. Peroxidase (POX; EC 1.11.1.7) activity increased under both salt concentrations in P. maritima, but only under 200 mM NaCl in P. media. Confirming this, five POX activity bands were identified in leaves of P. maritima, but only two bands were determined in P. media. Malondialdehyde levels in the leaves increased under salt stress in P. media but showed no change and decreased in P. maritima at 100 and 200 mM NaCl, respectively. These results suggest that the salt-tolerant P. maritima showed a better protection mechanism against oxidative damage caused by salt stress by its higher induced activities of antioxidant enzymes than the salt-sensitive P. media. 相似文献
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Moulick K Ahn JH Zong H Rodina A Cerchietti L Gomes DaGama EM Caldas-Lopes E Beebe K Perna F Hatzi K Vu LP Zhao X Zatorska D Taldone T Smith-Jones P Alpaugh M Gross SS Pillarsetty N Ku T Lewis JS Larson SM Levine R Erdjument-Bromage H Guzman ML Nimer SD Melnick A Neckers L Chiosis G 《Nature chemical biology》2011,7(11):818-826
Most cancers are characterized by multiple molecular alterations, but identification of the key proteins involved in these signaling pathways is currently beyond reach. We show that the inhibitor PU-H71 preferentially targets tumor-enriched Hsp90 complexes and affinity captures Hsp90-dependent oncogenic client proteins. We have used PU-H71 affinity capture to design a proteomic approach that, when combined with bioinformatic pathway analysis, identifies dysregulated signaling networks and key oncoproteins in chronic myeloid leukemia. The identified interactome overlaps with the well-characterized altered proteome in this cancer, indicating that this method can provide global insights into the biology of individual tumors, including primary patient specimens. In addition, we show that this approach can be used to identify previously uncharacterized oncoproteins and mechanisms, potentially leading to new targeted therapies. We further show that the abundance of the PU-H71-enriched Hsp90 species, which is not dictated by Hsp90 expression alone, is predictive of the cell's sensitivity to Hsp90 inhibition. 相似文献
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Metazoan Scc4 homologs link sister chromatid cohesion to cell and axon migration guidance 总被引:2,自引:0,他引:2 下载免费PDF全文
Seitan VC Banks P Laval S Majid NA Dorsett D Rana A Smith J Bateman A Krpic S Hostert A Rollins RA Erdjument-Bromage H Tempst P Benard CY Hekimi S Newbury SF Strachan T 《PLoS biology》2006,4(8):e242
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Hediye Acun-Bucht Ebru Tuncay Emin Darendeliler Gönül Kemikler 《Reports of Practical Oncology and Radiotherapy》2018,23(4):242-250