The tetraspanin TSP3 of Neurospora crassa is a vacuolar membrane protein and shares characteristics with IDI proteins

Mycologia ◽  
2016 ◽  
Vol 108 (3) ◽  
pp. 581-589
Author(s):  
Daniela Heine ◽  
Linda Petereit ◽  
Marcel R. Schumann ◽  
Diana Patzelt ◽  
Leila Rachid ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Neurospora Crassa ◽  
Vacuolar Membrane

scholarly journals Membrane recruitment of Atg8 by Hfl1 facilitates turnover of vacuolar membrane proteins in yeast cells approaching stationary phase

BMC Biology ◽  
2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Cheng-Wen He ◽  
Xue-Fei Cui ◽  
Shao-Jie Ma ◽  
Qin Xu ◽  
Yan-Peng Ran ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Stationary Phase ◽  
Molecular Mechanisms ◽  
Multivesicular Body ◽  
Degradation Process ◽  
Vacuolar Membrane ◽  
Yeast Cells ◽  
Membrane Structures ◽  
Membrane Recruitment

Abstract Background The vacuole/lysosome is the final destination of autophagic pathways, but can also itself be degraded in whole or in part by selective macroautophagic or microautophagic processes. Diverse molecular mechanisms are involved in these processes, the characterization of which has lagged behind those of ATG-dependent macroautophagy and ESCRT-dependent endosomal multivesicular body pathways. Results Here we show that as yeast cells gradually exhaust available nutrients and approach stationary phase, multiple vacuolar integral membrane proteins with unrelated functions are degraded in the vacuolar lumen. This degradation depends on the ESCRT machinery, but does not strictly require ubiquitination of cargos or trafficking of cargos out of the vacuole. It is also temporally and mechanistically distinct from NPC-dependent microlipophagy. The turnover is facilitated by Atg8, an exception among autophagy proteins, and an Atg8-interacting vacuolar membrane protein, Hfl1. Lack of Atg8 or Hfl1 led to the accumulation of enlarged lumenal membrane structures in the vacuole. We further show that a key function of Hfl1 is the membrane recruitment of Atg8. In the presence of Hfl1, lipidation of Atg8 is not required for efficient cargo turnover. The need for Hfl1 can be partially bypassed by blocking Atg8 delipidation. Conclusions Our data reveal a vacuolar membrane protein degradation process with a unique dependence on vacuole-associated Atg8 downstream of ESCRTs, and we identify a specific role of Hfl1, a protein conserved from yeast to plants and animals, in membrane targeting of Atg8.

scholarly journals Deletion ofPlasmodium falciparumProtein RON3 Affects the Functional Translocation of Exported Proteins and Glucose Uptake

mBio ◽  
2019 ◽  
Vol 10 (4) ◽  
Author(s):  
Leanne M. Low ◽  
Yvonne Azasi ◽  
Emma S. Sherling ◽  
Matthias Garten ◽  
Joshua Zimmerberg ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Glucose Uptake ◽  
Protein Transport ◽  
Dense Granule ◽  
Vacuolar Membrane ◽  
Malarial Parasite ◽  
Membrane Protein Complex ◽  
Erythrocyte Surface ◽  
Dependent Transport ◽  
Rhoptry Protein

ABSTRACTThe survival ofPlasmodiumspp. within the host red blood cell (RBC) depends on the function of a membrane protein complex, termed thePlasmodiumtranslocon of exported proteins (PTEX), that exports certain parasite proteins, collectively referred to as the exportome, across the parasitophorous vacuolar membrane (PVM) that encases the parasite in the host RBC cytoplasm. The core of PTEX consists of three proteins: EXP2, PTEX150, and the HSP101 ATPase; of these three proteins, only EXP2 is a membrane protein. Studying the PTEX-dependent transport of members of the exportome, we discovered that exported proteins, such as ring-infected erythrocyte surface antigen (RESA), failed to be transported in parasites in which the parasite rhoptry protein RON3 was conditionally disrupted. RON3-deficient parasites also failed to develop beyond the ring stage, and glucose uptake was significantly decreased. These findings provide evidence that RON3 influences two translocation functions, namely, transport of the parasite exportome through PTEX and the transport of glucose from the RBC cytoplasm to the parasitophorous vacuolar (PV) space where it can enter the parasite via the hexose transporter (HT) in the parasite plasma membrane.IMPORTANCEThe malarial parasite within the erythrocyte is surrounded by two membranes.Plasmodiumtranslocon of exported proteins (PTEX) in the parasite vacuolar membrane critically transports proteins from the parasite to the erythrocytic cytosol and membrane to create protein infrastructure important for virulence. The components of PTEX are stored within the dense granule, which is secreted from the parasite during invasion. We now describe a protein, RON3, from another invasion organelle, the rhoptry, that is also secreted during invasion. We find that RON3 is required for the protein transport function of the PTEX and for glucose transport from the RBC cytoplasm to the parasite, a function thought to be mediated by PTEX component EXP2.

scholarly journals Vba4p, a vacuolar membrane protein, is involved in the drug resistance and vacuolar morphology ofSaccharomyces cerevisiae

2015 ◽  
Vol 80 (2) ◽  
pp. 279-287 ◽  
Author(s):  
Miyuki Kawano-Kawada ◽  
Pongsanat Pongcharoen ◽  
Rieko Kawahara ◽  
Mayu Yasuda ◽  
Takashi Yamasaki ◽  
...  
Keyword(s):  
Drug Resistance ◽  
Membrane Protein ◽  
Vacuolar Membrane

scholarly journals Plasma Membrane Protein Nce102 Modulates Morphology and Function of the Yeast Vacuole

Biomolecules ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 1476
Author(s):  
Katarina Vaskovicova ◽  
Petra Vesela ◽  
Jakub Zahumensky ◽  
Dagmar Folkova ◽  
Maria Balazova ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Vacuolar Membrane ◽  
Yeast Culture ◽  
Membrane Domains ◽  
Biological Functions ◽  
Plasma Membrane Protein ◽  
Cell Architecture ◽  
And Function

Membrane proteins are targeted not only to specific membranes in the cell architecture, but also to distinct lateral microdomains within individual membranes to properly execute their biological functions. Yeast tetraspan protein Nce102 has been shown to migrate between such microdomains within the plasma membrane in response to an acute drop in sphingolipid levels. Combining microscopy and biochemistry methods, we show that upon gradual ageing of a yeast culture, when sphingolipid demand increases, Nce102 migrates from the plasma membrane to the vacuole. Instead of being targeted for degradation it localizes to V-ATPase-poor, i.e., ergosterol-enriched, domains of the vacuolar membrane, analogous to its plasma membrane localization. We discovered that, together with its homologue Fhn1, Nce102 modulates vacuolar morphology, dynamics, and physiology. Specifically, the fusing of vacuoles, accompanying a switch of fermenting yeast culture to respiration, is retarded in the strain missing both proteins. Furthermore, the absence of either causes an enlargement of ergosterol-rich vacuolar membrane domains, while the vacuoles themselves become smaller. Our results clearly show decreased stability of the V-ATPase in the absence of either Nce102 or Fhn1, a possible result of the disruption of normal microdomain morphology of the vacuolar membrane. Therefore, the functionality of the vacuole as a whole might be compromised in these cells.

scholarly journals Structure and Distribution of Organelles and Cellular Location of Calcium Transporters in Neurospora crassa

2009 ◽  
Vol 8 (12) ◽  
pp. 1845-1855 ◽  
Author(s):  
Barry J. Bowman ◽  
Marija Draskovic ◽  
Michael Freitag ◽  
Emma Jean Bowman
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Neurospora Crassa ◽  
Fluorescent Protein ◽  
Protein A ◽  
Vacuolar Membrane ◽  
Red Fluorescent Protein ◽  
Animal Cells ◽  
Marker Proteins ◽  
Hyphal Tip

ABSTRACT We wanted to examine the cellular locations of four Neurospora crassa proteins that transport calcium. However, the structure and distribution of organelles in live hyphae of N. crassa have not been comprehensively described. Therefore, we made recombinant genes that generate translational fusions of putative organellar marker proteins with green or red fluorescent protein. We observed putative endoplasmic reticulum proteins, encoded by grp-78 and dpm, in the nuclear envelope and associated membranes. Proteins of the vacuolar membrane, encoded by vam-3 and vma-1, were in an interconnected network of small tubules and vesicles near the hyphal tip, while in more distal regions they were in large and small spherical vacuoles. Mitochondria, visualized with tagged ARG-4, were abundant in all regions of the hyphae. Similarly, we tagged the four N. crassa proteins that transport calcium with green or red fluorescent protein to examine their cellular locations. NCA-1 protein, a homolog of the SERCA-type Ca2+-ATPase of animal cells, colocalized with the endoplasmic reticulum markers. The NCA-2 and NCA-3 proteins are homologs of Ca2+-ATPases in the vacuolar membrane in yeast or in the plasma membrane in animal cells. They colocalized with markers in the vacuolar membrane, and they also occurred in the plasma membrane in regions of the hyphae more than 1 mm from the tip. The cax gene encodes a Ca2+/H+ exchange protein found in vacuoles. As expected, the CAX protein localized to the vacuolar compartment. We observed, approximately 50 to 100 μm from the tip, a few spherical organelles that had high amounts of tagged CAX protein and tagged subunits of the vacuolar ATPase (VMA-1 and VMA-5). We suggest that this organelle, not described previously in N. crassa, may have a role in sequestering calcium.

scholarly journals Making two organelles from one: Woronin body biogenesis by peroxisomal protein sorting

2008 ◽  
Vol 180 (2) ◽  
pp. 325-339 ◽  
Author(s):  
Fangfang Liu ◽  
Seng Kah Ng ◽  
Yanfen Lu ◽  
Wilson Low ◽  
Julian Lai ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Neurospora Crassa ◽  
Filamentous Fungi ◽  
Dense Core ◽  
Cell Cortex ◽  
Protein Matrix ◽  
Woronin Body ◽  
Membrane Bound ◽  
And Control ◽  
Dual Functions

Woronin bodies (WBs) are dense-core organelles that are found exclusively in filamentous fungi and that seal the septal pore in response to wounding. These organelles consist of a membrane-bound protein matrix comprised of the HEX protein and, although they form from peroxisomes, their biogenesis is poorly understood. In Neurospora crassa, we identify Woronin sorting complex (WSC), a PMP22/MPV17-related membrane protein with dual functions in WB biogenesis. WSC localizes to large peroxisome membranes where it self-assembles into detergent-resistant oligomers that envelop HEX assemblies, producing asymmetrical nascent WBs. In a reaction requiring WSC, these structures are delivered to the cell cortex, which permits partitioning of the nascent WB and WB inheritance. Our findings suggest that WSC and HEX collaborate and control distinct aspects of WB biogenesis and that cortical association depends on WSC, which in turn depends on HEX. This dependency helps order events across the organellar membrane, permitting the peroxisome to produce a second organelle with a distinct composition and intracellular distribution.

scholarly journals Vacuolar protein Tag1 and Atg1–Atg13 regulate autophagy termination during persistent starvation in S. cerevisiae

2021 ◽  
Vol 134 (4) ◽  
pp. jcs253682
Author(s):  
Shintaro Kira ◽  
Masafumi Noguchi ◽  
Yasuhiro Araki ◽  
Yu Oikawa ◽  
Tamotsu Yoshimori ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Membrane Protein ◽  
Nitrogen Starvation ◽  
Genetic Screen ◽  
Vacuolar Membrane ◽  
Phagophore Assembly Site ◽  
Vacuolar Protein ◽  
Assembly Site ◽  
Starvation Conditions

ABSTRACTUnder starvation conditions, cells degrade their own components via autophagy in order to provide sufficient nutrients to ensure their survival. However, even if starvation persists, the cell is not completely degraded through autophagy, implying the existence of some kind of termination mechanism. In the yeast Saccharomyces cerevisiae, autophagy is terminated after 10–12 h of nitrogen starvation. In this study, we found that termination is mediated by re-phosphorylation of Atg13 by the Atg1 protein kinase, which is also affected by PP2C phosphatases, and the eventual dispersion of the pre-autophagosomal structure, also known as the phagophore assembly site (PAS). In a genetic screen, we identified an uncharacterized vacuolar membrane protein, Tag1, as a factor responsible for the termination of autophagy. Re-phosphorylation of Atg13 and eventual PAS dispersal were defective in the Δtag1 mutant. The vacuolar luminal domain of Tag1 and autophagic progression are important for the behaviors of Tag1. Together, our findings reveal the mechanism and factors responsible for termination of autophagy in yeast.

scholarly journals Transport of Metal-binding Peptides by HMT1, A Fission Yeast ABC-type Vacuolar Membrane Protein

1995 ◽  
Vol 270 (9) ◽  
pp. 4721-4728 ◽  
Author(s):  
Daniel F. Ortiz ◽  
Theresa Ruscitti ◽  
Kent F. McCue ◽  
David W. Ow
Keyword(s):  
Membrane Protein ◽  
Fission Yeast ◽  
Metal Binding ◽  
Vacuolar Membrane ◽  
Metal Binding Peptides ◽  
Binding Peptides

Vba2p, A Vacuolar Membrane Protein Involved in Basic Amino Acid Transport in Schizosaccharomyces pombe

2010 ◽  
Vol 74 (10) ◽  
pp. 2166-2169 ◽  
Author(s):  
Naoko SUGIMOTO ◽  
Tomoko IWAKI ◽  
Soracom CHARDWIRIYAPREECHA ◽  
Masamitsu SHIMAZU ◽  
Takayuki SEKITO ◽  
...  
Keyword(s):  
Amino Acid ◽  
Membrane Protein ◽  
Schizosaccharomyces Pombe ◽  
Amino Acid Transport ◽  
Basic Amino Acid ◽  
Vacuolar Membrane ◽  
Acid Transport
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