scholarly journals First person – Bishal Basak

Biology Open ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. bio058657
Keyword(s):  
Biological Sciences ◽  
Lipid Transfer Protein ◽  
Vesicular Trafficking ◽  
Early Career ◽  
First Person ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Contact Sites ◽  
Interdomain Interactions ◽  
Selection Of

ABSTRACTFirst Person is a series of interviews with the first authors of a selection of papers published in Biology Open, helping early-career researchers promote themselves alongside their papers. Bishal Basak is first author on ‘Interdomain interactions regulate the localization of a lipid transfer protein at ER-PM contact sites’, published in BiO. Bishal is a PhD student in the lab of Professor Raghu Padinjat at National Center for Biological Sciences, Rajiv Gandhi Nagar, Kodigehalli, Bengaluru, Karnataka, India, investigating non-vesicular trafficking of lipids at interorganeller contact sites regulate cellular physiology.

scholarly journals Interdomain interactions regulate the localization of a lipid transfer protein at ER-PM contact sites

2020 ◽  
Author(s):  
Bishal Basak ◽  
Harini Krishnan ◽  
Padinjat Raghu
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Transfer Protein ◽  
Intramolecular Interaction ◽  
Lipid Transfer ◽  
Loss Of Function ◽  
Transfer Protein ◽  
Contact Sites ◽  
Accurate Localization ◽  
Phosphatidylinositol Transfer ◽  
Interdomain Interactions

Abstract During phospholipase C-β (PLC-β) signalling in Drosophila photoreceptors, the phosphatidylinositol transfer protein (PITP) RDGB, is required for lipid transfer at endoplasmic reticulum (ER)-plasma membrane (PM) contact sites (MCS). Depletion of RDGB or its mis-localization away from the ER-PM MCS results in multiple defects in photoreceptor function. Previously, the interaction between the FFAT motif of RDGB and the integral ER protein dVAP-A was shown to be essential for accurate localization to ER-PM MCS. Here, we report that the FFAT/dVAP-A interaction alone is insufficient to localize RDGB accurately; this also requires the function of the C-terminal domains, DDHD and LNS2. Mutations in each of these domains results in mis-localization of RDGB leading to loss of function. While the LNS2 domain is necessary, it is not sufficient for the correct localization of RDGB, which also requires the C-terminal DDHD domain. The function of the DDHD domain is mediated through an intramolecular interaction with the LNS2 domain. Thus, interactions between the additional domains in a multi-domain PITP together lead to accurate localization at the MCS and signalling function.

scholarly journals Interdomain interactions regulate the localization of a lipid transfer protein at ER-PM contact sites

Biology Open ◽  
2021 ◽  
Vol 10 (3) ◽  
Author(s):  
Bishal Basak ◽  
Harini Krishnan ◽  
Padinjat Raghu
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Transfer Protein ◽  
Intramolecular Interaction ◽  
Lipid Transfer ◽  
Loss Of Function ◽  
Transfer Protein ◽  
Contact Sites ◽  
Accurate Localization ◽  
Phosphatidylinositol Transfer ◽  
Interdomain Interactions

ABSTRACT During phospholipase C-β (PLC-β) signalling in Drosophila photoreceptors, the phosphatidylinositol transfer protein (PITP) RDGB, is required for lipid transfer at endoplasmic reticulum (ER)–plasma membrane (PM) contact sites (MCS). Depletion of RDGB or its mis-localization away from the ER–PM MCS results in multiple defects in photoreceptor function. Previously, the interaction between the FFAT motif of RDGB and the integral ER protein dVAP-A was shown to be essential for accurate localization to ER–PM MCS. Here, we report that the FFAT/dVAP-A interaction alone is insufficient to localize RDGB accurately; this also requires the function of the C-terminal domains, DDHD and LNS2. Mutations in each of these domains results in mis-localization of RDGB leading to loss of function. While the LNS2 domain is necessary, it is not sufficient for the correct localization of RDGB, which also requires the C-terminal DDHD domain. The function of the DDHD domain is mediated through an intramolecular interaction with the LNS2 domain. Thus, interactions between the additional domains in a multi-domain PITP together lead to accurate localization at the MCS and signalling function. This article has an associated First Person interview with the first author of the paper.

scholarly journals First person – Wei Sheng Yap

2020 ◽  
Vol 133 (21) ◽  
pp. jcs256016
Keyword(s):  
Biological Sciences ◽  
Membrane Lipid ◽  
Early Career ◽  
Lipid Homeostasis ◽  
First Person ◽  
Early Career Researchers ◽  
Technological University ◽  
Selection Of

ABSTRACTFirst Person is a series of interviews with the first authors of a selection of papers published Journal of Cell Science, helping early-career researchers promote themselves alongside their papers. Wei Sheng Yap is first author on ‘The yeast FIT2 homologs are necessary to maintain cellular proteostasis and membrane lipid homeostasis’, published in JCS. Wei Sheng works in the lab of Guillaume Thibault in the School of Biological Sciences, Nanyang Technological University, Singapore, studying the interplay between the proteostasis network and lipid homeostasis.

scholarly journals Calcium-stimulated disassembly of focal adhesions mediated by an ORP3/IQSec1 complex

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Ryan S D'Souza ◽  
Jun Y Lim ◽  
Alper Turgut ◽  
Kelly Servage ◽  
Junmei Zhang ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Migration ◽  
Calcium Channels ◽  
Lipid Transfer Protein ◽  
Calcium Influx ◽  
Focal Adhesions ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Contact Sites ◽  
Lipid Exchange

Coordinated assembly and disassembly of integrin-mediated focal adhesions (FAs) is essential for cell migration. Many studies have shown that FA disassembly requires Ca2+ influx, however our understanding of this process remains incomplete. Here, we show that Ca2+ influx via STIM1/Orai1 calcium channels, which cluster near FAs, leads to activation of the GTPase Arf5 via the Ca2+-activated GEF IQSec1, and that both IQSec1 and Arf5 activation are essential for adhesion disassembly. We further show that IQSec1 forms a complex with the lipid transfer protein ORP3, and that Ca2+ influx triggers PKC-dependent translocation of this complex to ER/plasma membrane (PM) contact sites adjacent to FAs. In addition to allosterically activating IQSec1, ORP3 also extracts PI4P from the PM, in exchange for phosphatidylcholine. ORP3-mediated lipid exchange is also important for FA turnover. Together, these findings identify a new pathway that links calcium influx to FA turnover during cell migration.

scholarly journals First person – Matthew Zdradzinski

2021 ◽  
Vol 134 (7) ◽  
Keyword(s):  
Biological Sciences ◽  
South Carolina ◽  
Axon Growth ◽  
Mrna Localization ◽  
Early Career ◽  
First Person ◽  
University Of South Carolina ◽  
Early Career Researchers ◽  
Mrna Isoform ◽  
Selection Of

ABSTRACT First Person is a series of interviews with the first authors of a selection of papers published in Journal of Cell Science, helping early-career researchers promote themselves alongside their papers. Matthew Zdradzinski is co-first author on ‘Selective axonal translation of the mRNA isoform encoding prenylated Cdc42 supports axon growth’, published in JCS. Matthew is a PhD Student in the lab of Jeffery Twiss at the Department of Biological Sciences, University of South Carolina, Columbia, SC, where he is interested in neurobiology, focused around mRNA localization and its effects on axon growth, development and regeneration.

scholarly journals ORP5 regulates PI(4)P on the lipid droplet: Novel players on the monolayer

2019 ◽  
Vol 219 (1) ◽  
Author(s):  
Mike F. Renne ◽  
Brooke M. Emerling
Keyword(s):  
Lipid Droplet ◽  
Lipid Composition ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Contact Sites ◽  
Phosphatidylinositol 4

How the distinct lipid composition of organelles is determined and maintained is still poorly understood. In this issue, Du et al. (2019. J. Cell Biol.https://doi.org/10.1083/jcb.201905162) show that the lipid transfer protein ORP5 functions at ER–LD contact sites, regulating lipid droplet levels of phosphatidylserine and phosphatidylinositol-4-phosphate.

scholarly journals First person – Zhong-Qiu Yu

2021 ◽  
Vol 134 (19) ◽  
Keyword(s):  
Biological Sciences ◽  
Protein Interactions ◽  
Visual Detection ◽  
Early Career ◽  
Degradation Pathways ◽  
First Person ◽  
Early Career Researchers ◽  
Research Associate ◽  
Beijing China ◽  
Selection Of

ABSTRACT First Person is a series of interviews with the first authors of a selection of papers published in Journal of Cell Science, helping early-career researchers promote themselves alongside their papers. Zhong-Qiu Yu is first author on ‘ Visual detection of binary, ternary and quaternary protein interactions in fission yeast using a Pil1 co-tethering assay’, published in JCS. Zhong-Qiu conducted the research described in this article while a postdoc in Li-Lin Du's lab at National Institute of Biological Sciences, Beijing, China. He is now a research associate in the lab of David Rubinsztein at Department of Medical Genetics, Cambridge Institute for Medical Research, UK, investigating protein degradation pathways and neurodegeneration diseases.

scholarly journals First person – Takeshi Harada

2020 ◽  
Vol 133 (21) ◽  
pp. jcs256024
Keyword(s):  
Graduate School ◽  
Assistant Professor ◽  
Early Career ◽  
First Person ◽  
Contact Sites ◽  
Early Career Researchers ◽  
School Of Medicine ◽  
Mitochondrial Functions ◽  
Selection Of

ABSTRACTFirst Person is a series of interviews with the first authors of a selection of papers published in Journal of Cell Science, helping early-career researchers promote themselves alongside their papers. Takeshi Harada is first author on ‘Palmitoylated CKAP4 regulates mitochondrial functions through an interaction with VDAC2 at ER–mitochondria contact sites’, published in JCS. Takeshi is an assistant professor in the lab of Akira Kikuchi at the Graduate School of Medicine, Osaka University, Japan, investigating the role of CKAP4 at ER–mitochondria contact sites.

scholarly journals PR-proteins as markers of winter wheat (Triticum aestivum L.) resistance to leaf pathogens

2019 ◽  
Vol 64 (3) ◽  
pp. 286-291 ◽  
Author(s):  
Y. V. Viazau ◽  
M. S. Radyuk ◽  
E. A. Filipchik ◽  
N. V. Shalygo
Keyword(s):  
Winter Wheat ◽  
Lipid Transfer Protein ◽  
Constitutive Expression ◽  
Triticum Aestivum L ◽  
Pcr Analysis ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Resistant Varieties ◽  
Genes Encoding ◽  
Selection Of

Using real-time PCR analysis, the constitutive expression of PR-protein genes encoding thaumatin-like protein (TLP), peroxidase III (TaPero), chitinase (Chitin), glucanase (Glucan), protease inhibitor (PrInh), oxalate oxidase (OxOxid) and lipid transfer protein (Ltp) was studied in collection varieties of winter wheat. It has been shown that plants of varieties with increased resistance to a complex of leaf pathogens have higher constitutive expression levels of Chitin and PrInh genes, and, to a greater extent, of TLP, TaPero and Glucan genes, compared with non-resistant varieties. It is proposed to use constitutive levels of expression of TLP, TaPero and Glucan genes for the selection of winter wheat varietal samples with increased resistance to the complex of leaf diseases.

scholarly journals Calcium-stimulated disassembly of focal adhesions mediated by an ORP3/IQSec1 complex

2019 ◽  
Author(s):  
RS D’Souza ◽  
JY Lim ◽  
A Turgut ◽  
K Servage ◽  
J Zhang ◽  
...  
Keyword(s):  
Cell Migration ◽  
Lipid Transfer Protein ◽  
Calcium Influx ◽  
Focal Adhesions ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Lipid Exchange ◽  
Membrane Contact

AbstractCoordinated assembly and disassembly of integrin-mediated focal adhesions (FAs) is essential for cell migration. Many studies have shown that FA disassembly requires Ca2+ influx, however our understanding of this process remains incomplete. Here we show that Ca2+ influx via STIM1/Orai1 calcium channels, which cluster near FAs, leads to activation of the GTPase Arf5 via the Ca2+-activated GEF IQSec1, and that both IQSec1 and Arf5 activation are essential for adhesion disassembly. We further show that IQSec1 forms a complex with the lipid transfer protein ORP3, and that Ca2+ influx triggers PKC-dependent translocation of this complex to ER/plasma membrane contact sites adjacent to FAs. In addition to allosterically activating IQSec1, ORP3 also extracts PI4P from the PM, in exchange for phosphatidylcholine. ORP3-mediated lipid exchange is also important for FA turnover. Together, these findings identify a new pathway that links calcium influx to FA turnover during cell migration.

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