scholarly journals Role of membrane contact sites in protein import into mitochondria

2015 ◽  
Vol 24 (3) ◽  
pp. 277-297 ◽  
Author(s):  
Susanne E. Horvath ◽  
Heike Rampelt ◽  
Silke Oeljeklaus ◽  
Bettina Warscheid ◽  
Martin van der Laan ◽  
...  
Keyword(s):  
Protein Import ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Membrane Contact

The role of membrane contact sites at the bacteria-host interface

2021 ◽  
pp. 1-13
Author(s):  
Chen Jiang ◽  
Xue Huang ◽  
Jia Yao ◽  
Lihua Yu ◽  
Fujing Wei ◽  
...  
Keyword(s):  
Membrane Contact Sites ◽  
Contact Sites ◽  
Membrane Contact

scholarly journals A VPS13D spastic ataxia mutation disrupts the conserved adaptor binding site in yeast Vps13

2019 ◽  
Author(s):  
Samantha K. Dziurdzik ◽  
Björn D. M. Bean ◽  
Michael Davey ◽  
Elizabeth Conibear
Keyword(s):  
Binding Site ◽  
Neurological Disorders ◽  
Membrane Recruitment ◽  
Spastic Ataxia ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Membrane Contact ◽  
Asparagine Residue ◽  
Early Onset Parkinson’S Disease

AbstractMutations in each of the four human VPS13 (VPS13A-D) proteins are associated with distinct neurological disorders: chorea-acanthocytosis, Cohen syndrome, early-onset Parkinson’s disease and spastic ataxia. Recent evidence suggests that the different VPS13 paralogs transport lipids between organelles at different membrane contact sites. How each VPS13 isoform is targeted to organelles is not known. We have shown that the localization of yeast Vps13 protein to membranes requires a conserved six-repeat region, the Vps13 Adaptor Binding (VAB) domain, which binds to organelle-specific adaptors. Here, we use a systematic mutagenesis strategy to determine the role of each repeat in recognizing each known adaptor. Our results show that mutation of invariant asparagines in repeats 1 and 6 strongly impact the binding all adaptors and block Vps13 membrane recruitment. However, we find that repeats 5 to 6 are sufficient for localization and interaction with adaptors. This supports a model where a single adaptor binding site is found in the last two repeats of the VAB domain, while VAB domain repeat 1 may help maintain domain conformation. Importantly, a disease-causing mutation in VPS13D, which maps to the highly conserved asparagine residue in repeat 6, blocks adaptor binding and Vps13 membrane recruitment when modeled in yeast. Our findings are consistent with a conserved adaptor binding role for the VAB domain and suggests the presence of as-yet-unidentified adaptors in both yeast and humans.

scholarly journals The Vacuole and Mitochondria Patch (vCLAMP) Protein Mcp1 Is Involved in Maintenance of Mitochondrial Function and Mitophagy in Candida albicans

2021 ◽  
Vol 12 ◽  
Author(s):  
Xiaolong Mao ◽  
Li Yang ◽  
Yiming Fan ◽  
Jiazhen Wang ◽  
Dongkai Cui ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Carbon Sources ◽  
Cellular Functions ◽  
Core Component ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Mitochondrial Functions ◽  
Abnormal Accumulation ◽  
Membrane Contact

The vacuole and mitochondria patches (vCLAMPs) are novel membrane contact sites in yeast. However, their role in autophagy has not been elucidated so far. In this article, the role of Mcp1, one core component of vCLAMP, in mitophagy of Candida albicans was investigated. Deletion of MCP1 led to abnormal accumulation of enlarged mitochondria and attenuated stability of mitochondrial DNA (mtDNA) in C. albicans when cultured in non-fermentable carbon sources. Furthermore, the mcp1Δ/Δ mutant exhibited defective growth and degradation of Csp37-GFP. These results indicate that Mcp1 plays a crucial role in mitophagy and maintenance of mitochondrial functions under the non-fermentable condition. Interestingly, this deletion had no impact on degradation of Atg8 (the macroautophagy reporter) and Lap41 (the cytoplasm-to-vacuole targeting pathway marker) under SD-N medium. Moreover, deletion of MCP1 inhibited filamentous growth and impaired virulence of the pathogen. This study provides an insight to vCLAMPs in cellular functions and pathogenicity in C. albicans.

scholarly journals VPS13D interacts with VCP/p97 and negatively regulates ER- mitochondrial interactions

2021 ◽  
pp. mbc.E21-03-0097
Author(s):  
Yuanjiao Du ◽  
Jingru Wang ◽  
Juan Xiong ◽  
Na Fang ◽  
Wei-Ke Ji
Keyword(s):  
Negative Regulation ◽  
Mitochondrial Morphology ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Cellular Events ◽  
Membrane Contact ◽  
The Stability ◽  
Vacuolar Protein ◽  
Mitochondrial Dna Synthesis

Membrane contact sites (MCSs) between the endoplasmic reticulum (ER) and mitochondria are emerging as critical hubs for diverse cellular events, and alterations in the extent of these contacts are linked to neurodegenerative diseases. However, the mechanisms that control ER-mitochondrial interactions are so far elusive. Here, we demonstrate a key role of vacuolar protein sorting-associated protein 13D (VPS13D) in the negative regulation of ER-mitochondrial MCSs. VPS13D suppression results in extensive ER-mitochondrial tethering, a phenotype that can be substantially rescued by suppression of the tethering proteins VAPB and PTPIP51. VPS13D interacts with valosin-containing protein (VCP/p97) to control the level of ER-resident VAPB at contacts. VPS13D is required for the stability of p97. Functionally, VPS13D suppression leads to severe defects in the mitochondrial morphology, mitochondrial cellular distribution and mitochondrial DNA synthesis. Together our results suggest that VPS13D negatively regulates the ER-mitochondrial MCSs partially through its interactions with VCP/p97. [Media: see text]

scholarly journals The Drosophila photoreceptor as a model system for studying signalling at membrane contact sites

2016 ◽  
Vol 44 (2) ◽  
pp. 447-451 ◽  
Author(s):  
Shweta Yadav ◽  
Shamshad Cockcroft ◽  
Padinjat Raghu
Keyword(s):  
Membrane Composition ◽  
Contact Site ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Physiological Processes ◽  
Specific Proteins ◽  
Intracellular Organelles ◽  
Membrane Contact ◽  
Cellular Compartments

Several recent studies have demonstrated the existence of membrane contact sites (MCS) between intracellular organelles in eukaryotic cells. Recent exciting studies have also demonstrated the existence of biomolecular interactions at these contact sites in mediating changes in the membrane composition of the cellular compartments. However, the role of such contact sites in regulating organelle function and physiological processes remains less clear. In this review we discuss the existence of a contact site between the plasma membrane (PM) and the endoplasmic reticulum (ER) in Drosophila photoreceptors. Further, we discuss the role of specific proteins present at this location in regulating phospholipid turnover and its impact in regulating a physiological process, namely phototransduction.

scholarly journals Role of membrane contact sites in PM ‐ ER sterol transport (606.7)

2014 ◽  
Vol 28 (S1) ◽  
Author(s):  
Yves Sere ◽  
Jesper Johansen ◽  
Christopher Beh ◽  
Anant Menon
Keyword(s):  
Membrane Contact Sites ◽  
Contact Sites ◽  
Sterol Transport ◽  
Membrane Contact

scholarly journals Octameric mitochondrial creatine kinase induces and stabilizes contact sites between the inner and outer membrane

2005 ◽  
Vol 385 (2) ◽  
pp. 445-450 ◽  
Author(s):  
Oliver SPEER ◽  
Nils BÄCK ◽  
Tanja BUERKLEN ◽  
Dieter BRDICZKA ◽  
Alan KORETSKY ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Transgenic Mice ◽  
Outer Membrane ◽  
Liver Mitochondria ◽  
Wild Type ◽  
Mitochondrial Creatine Kinase ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Membrane Contact

We have investigated the role of the protein ubiquitous mitochondrial creatine kinase (uMtCK) in the formation and stabilization of inner and outer membrane contact sites. Using liver mitochondria isolated from transgenic mice, which, unlike control animals, express uMtCK in the liver, we found that the enzyme was associated with the mitochondrial membranes and, in addition, was located in membrane-coated matrix inclusions. In mitochondria isolated from uMtCK transgenic mice, the number of contact sites increased 3-fold compared with that observed in control mitochondria. Furthermore, uMtCK-containing mitochondria were more resistant to detergent-induced lysis than wild-type mitochondria. We conclude that octameric uMtCK induces the formation of mitochondrial contact sites, leading to membrane cross-linking and to an increased stability of the mitochondrial membrane architecture.

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