{"title":"Editorial: (for \"Contact\" (CTC) journal).","authors":"Timothy P Levine","doi":"10.1177/2515256418771770","DOIUrl":"https://doi.org/10.1177/2515256418771770","url":null,"abstract":"“Contact” is a word with many connotations, from the personal to business. Here, it refers to the highly specialised world of membrane contact sites. In 2018, that meaning is clear to cell biologists, and people in related disciplines where it would not have been in 2008. The journal is dedicated to describing all aspects of the sites inside cells where different organelles interact (contact) with each other. This is the first journal for this field, which is still so young that we have no complete consensus on any of its most basic terms. For instance, it says above that the journal is about membrane contact sites, and that is the most recognisable phrase for this topic, but it is not the most accurate. If you read the ground breaking work of Maya Schuldiner’s group on contact between one organelle with half a membrane and another with none at all [1], you might agree we should drop the “membrane” part, though with just “contact sites”, our field would be even more likely to be misunderstood by non-scientists.","PeriodicalId":10556,"journal":{"name":"Contact (Thousand Oaks (Ventura County, Calif.))","volume":"1 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1177/2515256418771770","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36578950","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Endoplasmic Reticulum-Vacuole Contact Sites \"Bloom\" With Stress-Induced Lipid Droplets.","authors":"W Mike Henne, Hanaa Hariri","doi":"10.1177/2515256418756112","DOIUrl":"https://doi.org/10.1177/2515256418756112","url":null,"abstract":"<p><p>Lipid droplets (LDs) serve as specialized cytoplasmic organelles that harbor energy-rich lipids for long-term storage and may be mobilized as nutrient sources during extended starvation. How cells coordinate LD biogenesis and utilization in response to fluctuations in nutrient availability remains poorly understood. Here, we discuss our recent work revealing how yeast spatially organize LD budding at organelle contacts formed between the endoplasmic reticulum and yeast vacuole/lysosome (sites known as nucleus-vacuole junctions [NVJs]). During times of imminent nutrient exhaustion, we observe blooms of stress-induced LDs surrounding the NVJ and find that this LD clustering is regulated by NVJ-resident protein Mdm1. We also discuss several emerging studies revealing specific proteins that demarcate a subpopulation of NVJ-associated LDs. Collectively, these studies reveal a previously unappreciated role for the spatial compartmentalization of LDs at organelle contacts and highlight an important role for interorganellar cross talk in LD dynamics under times of nutritional stress.</p>","PeriodicalId":10556,"journal":{"name":"Contact (Thousand Oaks (Ventura County, Calif.))","volume":"1 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1177/2515256418756112","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36401822","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"ER-mitochondria contacts are required for pexophagy in <i>Saccharomyces cerevisiae</i>.","authors":"Xu Liu, Xin Wen, Daniel J Klionsky","doi":"10.1177/2515256418821584","DOIUrl":"https://doi.org/10.1177/2515256418821584","url":null,"abstract":"<p><p>Peroxisomes play important roles in lipid metabolism. Surplus or damaged peroxisomes can be selectively targeted for autophagic degradation, a process termed pexophagy. Maintaining a proper level of pexophagy is critical for cellular homeostasis. Here we found that endoplasmic reticulum (ER)-mitochondria contact sites are necessary for efficient pexophagy. During pexophagy, the peroxisomes destined for degradation are adjacent to the ER-mitochondria encounter structure (ERMES) that mediates formation of ER- mitochondria contacts; disruption of the ERMES results in a severe defect in pexophagy. We show that a mutant form of Mdm34, a component of the ERMES, which impairs ERMES formation and diminishes its association with the peroxisomal membrane protein Pex11, also leads to defects in pexophagy. The dynamin-related GTPase Vps1, which is specific for peroxisomal fission, is recruited to the peroxisomes at ER-mitochondria contacts by the selective autophagy scaffold Atg11 and the pexophagy receptor Atg36, facilitating peroxisome degradation.</p>","PeriodicalId":10556,"journal":{"name":"Contact (Thousand Oaks (Ventura County, Calif.))","volume":"2 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1177/2515256418821584","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37207182","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"In Close Proximity: The Lipid Droplet Proteome and Crosstalk With the Endoplasmic Reticulum.","authors":"Kirill Bersuker, James A Olzmann","doi":"10.1177/2515256418768996","DOIUrl":"https://doi.org/10.1177/2515256418768996","url":null,"abstract":"<p><p>Lipid droplets (LDs) are conserved, endoplasmic reticulum (ER)-derived organelles that act as a dynamic cellular repository for neutral lipids. Numerous studies have examined the composition of LD proteomes by using mass spectrometry to identify proteins present in biochemically isolated buoyant fractions that are enriched in LDs. Although many bona fide LD proteins were identified, high levels of non-LD proteins that contaminate buoyant fractions complicate the detection of true LD proteins. To overcome this problem, we recently developed a proximity-labeling proteomic method to define high-confidence LD proteomes. Moreover, employing this approach, we discovered that ER-associated degradation impacts the composition of LD proteomes by targeting select LD proteins for clearance by the 26S proteasome as they transit between the ER and LDs. These findings implicate the ER as a site of LD protein degradation and underscore the high degree of crosstalk between ER and LDs.</p>","PeriodicalId":10556,"journal":{"name":"Contact (Thousand Oaks (Ventura County, Calif.))","volume":"1 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1177/2515256418768996","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36389945","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Takanori Otomo, Saikat Chowdhury, Gabriel C Lander
{"title":"The rod-shaped ATG2A-WIPI4 complex tethers membranes in vitro.","authors":"Takanori Otomo, Saikat Chowdhury, Gabriel C Lander","doi":"10.1177/2515256418819936","DOIUrl":"https://doi.org/10.1177/2515256418819936","url":null,"abstract":"<p><p>The autophagosome precursor membrane, termed the \"isolation membrane\" or \"phagophore,\" emerges adjacent to a PI3P-enriched transient subdomain of the ER called the \"omegasome,\" thereafter expanding to engulf cytoplasmic content. Uncovering the molecular events that occur in the vicinity of the omegasome during phagophore biogenesis is imperative for understanding the mechanisms involved in this critical step of the autophagy pathway. We recently characterized the ATG2A-WIPI4 complex, one of the factors that localize to the omegasome and play a critical role in mediating phagophore expansion. Our structural and biochemical studies revealed that ATG2A is a rod-shaped protein with membrane-interacting properties at each end, endowing ATG2A with membrane-tethering capability. Association of the PI3P-binding protein WIPI4 at one of the ATG2A tips enables the ATG2A-WIPI4 complex to specifically tether PI3P-containing membranes to non-PI3P-containing membranes. We proposed models for the ATG2A-WIPI4 complex-mediated membrane associations between the omegasome and surrounding membranes, including the phagophore edge, the ER, ATG9 vesicles, and COPII vesicles.</p>","PeriodicalId":10556,"journal":{"name":"Contact (Thousand Oaks (Ventura County, Calif.))","volume":"1 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1177/2515256418819936","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36561485","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}