MOSPD2 tethers the ER to organelles bearing FFAT‐containing proteins

Slides:



Advertisements
Similar presentations
Common Evolutionary Origin for Coated Vesicles and Nuclear Pore Complexes Devos D, Dokudovskaya S, Alber F, Marti-Renom MA, Chait BT, Sali A, Rout MP UCSF.
Advertisements

ORGANELLES IN CELLULAR TRANSPORT Endoplasmic reticulum, Golgi apparatus, vesicles, cytoplasm. Warm-up Questions: What is the difference between active.
1.6 Parts of cell seen with an electron microscope.
MOSPD2 is an ER‐resident protein able to tether synthetic vesicles by binding the FFAT motif MOSPD2 is an ER‐resident protein able to tether synthetic.
Cell Organelles.
Representation of Adhesion GPCR interactions within the NTFs
Protein sequences and three‐dimensional structures of HUB1 (homologous to ubiquitin 1), ubiquitin and ubiquitin‐like modifiers. Protein sequences and three‐dimensional.
Yeast Tgl3p expressed in HeLa cells localizes to lipid droplets.
Nat. Rev. Nephrol. doi: /nrneph
The Mechanisms of Vesicle Budding and Fusion
Merlin and ERM protein domain organization and phosphoregulation.
TEK B.4B Concept: Investigate and Identify Cellular Processes Including Functions of Cellular Parts.
Important port for SHIP-1 at Dok-3
MOSPD2 recruitment to interorganelle contact sites depends on the interaction between the FFAT motif and the MSP domain MOSPD2 recruitment to interorganelle.
Location of IL‐17‐producing cell types.
The major protein‐translocation machineries in eukaryotic and prokaryotic cells. The major protein‐translocation machineries in eukaryotic and prokaryotic.
Recognition of double‐stranded telomeric DNA
Figure 1 The machinery of autophagy
MCM3AP‐mediated acetylation of MCM3.
Acid Test: Lipid Antigens Get into the Groove
Volume 29, Issue 5, Pages (November 2008)
A model for Mcl1 regulation of Bak‐dependent MOMP
Figure 3 The genomic organization and protein architecture of OCRL
F. Gisou van der Goot, Jean Gruenberg  Developmental Cell 
A Tether Is a Tether Is a Tether: Tethering at Membrane Contact Sites
Endogenous MOSPD2 is recruited to interorganelle contact sites by FFAT‐containing proteins Endogenous MOSPD2 is recruited to interorganelle contact sites.
VAP‐A is recruited to interorganelle contact sites together with MOSPD2 VAP‐A is recruited to interorganelle contact sites together with MOSPD2 AHeLa cells.
Tankyrase Loses Its Grip on SH3BP2 in Cherubism
Identification of MOSPD2, a new FFAT motif‐binding protein
Cholera 12 The American Journal of Medicine
Cellular Organelles Nucleus Nuclear Membrane Nucleolus
The MSP domain of MOSPD2 is sufficient to interact with STARD3 and STARD3NL The MSP domain of MOSPD2 is sufficient to interact with STARD3 and STARD3NL.
The FKBP8‐ATG8 interaction is dependent on an intact LIR docking site (LDS)‏ The FKBP8‐ATG8 interaction is dependent on an intact LIR docking site (LDS)
The production of reduced or oxidized glutathione can occur at various stages during the formation of native disulphide bonds. The production of reduced.
Catherine L. Jackson, Laurence Walch, Jean-Marc Verbavatz 
Sebastien Paillusson, Radu Stoica, Patricia Gomez-Suaga, Dawn H. W
The MSP domain of MOSPD2 binds the FFAT motif
MOSPD2 is a putative tail‐anchored protein
Hepatitis C virus–cell interactions and their role in pathogenesis
Membrane Fusion  Reinhard Jahn, Thorsten Lang, Thomas C Südhof  Cell 
ROUGH E.R By:ISAIAH HAIRSTON.
Endogenous MOSPD2 is recruited to interorganelle contact sites by FFAT‐containing proteins Endogenous MOSPD2 is recruited to interorganelle contact sites.
FFAT rescues VAPA-mediated inhibition of ER-to-golgi transport and VAPB-mediated ER aggregation By: Derek Prosser, Duvinh Tran, Pierre-Yves Gougeon, Carine.
FFAT motif‐dependent recruitment of MOSPD2 in ER–endosome contacts by STARD3NL FFAT motif‐dependent recruitment of MOSPD2 in ER–endosome contacts by STARD3NL.
From ER to Eph Receptors: New Roles for VAP Fragments
FFAT‐containing proteins recruit the ER‐resident MOSPD2 protein to interorganelle contact sites FFAT‐containing proteins recruit the ER‐resident MOSPD2.
Membrane Traffic: Trans-Golgi Tethers Leave a Surprisingly Small GAP
The MSP domain of MOSPD2 binds the FFAT motif with an affinity in the micromolar range The MSP domain of MOSPD2 binds the FFAT motif with an affinity in.
FFAT rescues VAPA-mediated inhibition of ER-to-golgi transport and VAPB-mediated ER aggregation By: Derek Prosser, Duvinh Tran, Pierre-Yves Gougeon, Carine.
REVIEW CELL ORGANELLES.
Transfer of Cholesterol by the NPC Team
Flavivirus particle assembly
The ER is the main source of cholesterol accumulated by STARD3 in endosomes The ER is the main source of cholesterol accumulated by STARD3 in endosomes.
MOSPD2 silencing affects interorganelle contact sites organization
Sequence alignment of PHCCEx domains with secondary structure elements of the Tiam2 PHCCEx domain at the top. Sequence alignment of PHCCEx domains with.
VAP protein knockdown abolishes STARD3‐mediated cholesterol accumulation in endosomes VAP protein knockdown abolishes STARD3‐mediated cholesterol accumulation.
Schematic diagram of the proposed structure of CFTR
Rik van der Kant, Lawrence S.B. Goldstein  Developmental Cell 
Structure of Yeast OSBP-Related Protein Osh1 Reveals Key Determinants for Lipid Transport and Protein Targeting at the Nucleus-Vacuole Junction  Mohammad.
Genomic Sequence Analysis of the Mouse Desmoglein Cluster Reveals Evidence for Six Distinct Genes: Characterization of Mouse DSG4, DSG5, and DSG6  Neil.
Localization of putative cholesterol-binding motifs in the homology model of human glucose transporter 1 (GLUT1) protein. Localization of putative cholesterol-binding.
Organelle crosstalk in the kidney
CD44 binding surface of the Tiam2 PHCCEx domain.
Figure 2 Autophagosome formation in mammalian cells
VAP protein knockdown abolishes STARD3‐mediated cholesterol accumulation in endosomes VAP protein knockdown abolishes STARD3‐mediated cholesterol accumulation.
Schoelz James E. , Harries Phillip A. , Nelson Richard S.  
Small G Protein Signaling in Neuronal Plasticity and Memory Formation: The Specific Role of Ras Family Proteins  Xiaojing Ye, Thomas J. Carew  Neuron 
Autophagosome Formation: Cutting the Gordian Knot at the ER
Pleckstrin Homology Domains: Two Halves Make a Hole?
ER MCSs with other organelles and the PM.
Presentation transcript:

MOSPD2 tethers the ER to organelles bearing FFAT‐containing proteins MOSPD2 tethers the ER to organelles bearing FFAT‐containing proteins Schematic representation of ER–endosome, ER–mitochondria, and ER–Golgi contacts involving MOSPD2 and a number of its interacting partners: STARD3NL, STARD3, ORP1L, PTPIP51, and STARD11. LE, late endosome; ER, endoplasmic reticulum; TM, transmembrane domain; MSP, Major Sperm Protein domain; FFAT, Two phenylalanines in an acidic tract motif [9], [26]; CRAL‐TRIO, cellular retinaldehyde‐binding protein and triple functional domain protein domain [48]; MENTAL, metastatic lymph node 64 N‐terminal domain, anchoring STARD3 and STARD3NL to the LE membrane [53], [65]; START, steroidogenic acute regulatory protein (StAR)‐related lipid Transfer domain; in STARD11 (CERT), the START domain is mediating ceramide transfer from the ER to the Golgi [70], and in STARD3, the START domain is involved in cholesterol transfer from the ER to LE (STARD3) [23]; PH, pleckstrin homology domain; this domain mediates the association of STARD11 with the Golgi membrane by interacting with PI(4)P; in ORP1L, it might also be involved in phosphoinositide binding‐mediated membrane interaction [51], [71]; ORD, oxysterol‐binding protein (OSBP)‐related domain [72]; AR, ankyrin repeat domain involved in the interaction with Rab7 at the LE membrane [51]; CC, coiled‐coil. Thomas Di Mattia et al. EMBO Rep. 2018;19:e45453 © as stated in the article, figure or figure legend