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Mintu Chandra

@mintuju.bsky.social
21 followers 31 following 8 posts

Structural biologist exploring protein structure-function relationships and their roles in membrane trafficking, uncovering critical molecular interactions within cellular membranes. He/Him. Research Assistant Professor, Vanderbilt University, USA.

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Reposted by Mintu Chandra
Mary Munson @marymunson4.bsky.social · 26/08/2026
Structural biology postdoctoral position open in my lab--apply now! For more information about the lab, see www.umassmed.edu/munsonlab/. Interested candidates should apply through the University of Massachusetts Chan Medical School jobs portal (www.ummsjobs.com/job/11668/).
umassmed.edu
Munson Lab | Home | BMB | UMass Chan Medical School
The Munson Lab researches the mechanistic basis for the regulation of spatial and temporal specificity in membrane trafficking in the Biochemistry & Molecular Biotechnology Department at UMass Chan Me...
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Cell Biology J-Club @cellclub.bsky.social · 13/08/2026
Reconstitution of multistep recruitment of ULK1 to membranes in autophagy www.biorxiv.org/content/10.1...
biorxiv.org
Reconstitution of multistep recruitment of ULK1 to membranes in autophagy
The Human ULK1 autophagy-initiating complex consists of ULK1, FIP200, and the HORMA domain heterodimer ATG13:ATG101. PI3P is essential to recruit ULK1C to membranes for ULK1, but ULK1C subunits do not...
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Reposted by Mintu Chandra
Misha Kudryashev @mishakudryashev.bsky.social · 01/08/2026
Take a look at our new paper on the structure of the EHD2 that, upon oligomerization, forms rings that remodel the plasma membrane and form caveolae. Beautiful work by Elena, Vasya @vasiliimikirtumov.bsky.social, Jeff & Oliver Dumke's team; take a look: www.nature.com/articles/s41...
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Juan S. Bonifacino @juanbonifacino.bsky.social · 23/07/2026
New study from our lab at NICHD, NIH! We identify TBC1D9 and TBC1D9B as novel ARL8 effectors that suppress exosome secretion by inactivating RAB11A and thus blocking exocyst-dependent fusion of multivesicular endosomes with the plasma membrane. www.pnas.org/doi/10.1073/...
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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · 12/01/2026
Happy to finally share the amazing results of our long-term collaboration with Karin Reinisch’s lab on how bridge lipid-transfer proteins (BLTPs) cooperate with partner proteins to orchestrate lipid delivery. A quick thread (1/7) www.biorxiv.org/content/10.6...
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Journal of Cell Biology @jcb.org · 21/05/2026
Chouhan, Phogat et al. of the Mahak Sharma lab report that the small GTP-binding protein Arl8b recruits the Rab11a GAP, TBC1D9B, to inactivate Rab11a-mediated recycling of newly synthesized LAMP1 and mediate its efficient sorting to #lysosomes. rupress.org/jcb/article/...
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Reposted by Mintu Chandra
Briggs Group @briggsgroup.bsky.social · 18/05/2026
The architecture of carriers formed by AP3:ARF1 for lysosomal membrane protein transport: www.science.org/doi/10.1126/.... Work from @jggkaufman.bsky.social, in collaboration with @dgershlick.bsky.social and David Owen. @mpibiochem.bsky.social @thecimr.bsky.social
science.org
Architecture of clathrin-independent AP3:ARF1-coated carriers
AP3 generates clathrin-free carriers on endosomes by organizing via ARF1 dimers into elongated membrane-deforming arrays.
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Mintu Chandra @mintuju.bsky.social · 26/04/2026
Excited to share our latest review article on how cells organize and transport important molecules! Grateful to collaborate with amazing colleagues on this work—check it out here: doi.org/10.1016/j.ce...
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Reposted by Mintu Chandra
Spang Lab @spanglab.bsky.social · 30/01/2026
Check out our newest findings on how #lysosomes are generated from #endolysosomes. Great work from @samit2104.bsky.social ! @biozentrum.unibas.ch , @unibas.ch #cellbio #cell #organelles Ca2+ and DRP1 drive endocytic lysosome reformation at tripartite contact sites www.biorxiv.org/content/10.6...
biorxiv.org
Ca2+ and DRP1 drive endocytic lysosome reformation at tripartite contact sites
Lysosomes are essential in maintaining cellular health. Endocytic lysosome reformation (ELR) regenerates functional lysosomes following degradation of endocytic cargo, yet the mechanisms driving this process remain largely unknown. Here, we define the molecular machinery underlying ELR. We find that unlike autophagic lysosome reformation (ALR), ELR proceeds independently of mTOR and dynamin 2, but requires the mitochondrial fission GTPase DRP1. DRP1 mediates scission of endolysosomal tubules at contact sites with the endoplasmic reticulum (ER) and mitochondria. Disruption of DRP1 function or ER endolysosome contact results in elongated tubules, indicating defective lysosome reformation. Moreover, mitochondrial activity is essential for tubule initiation, and Ca2+ transfer from endolysosomes to mitochondria is crucial for ELR onset. Our findings reveal a dual role for mitochondria in ELR: first in ELR initiation and second in DRP1-dependent tubule fission at ER-mitochondria-endolysosome tripartite contact sites, uncovering the previously unappreciated role of mitochondria in endolysosome remodeling and fission. ### Competing Interest Statement The authors have declared no competing interest. Swiss National Science Foundation, 320030-231859, 310030-197779 University of Basel, https://ror.org/02s6k3f65
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Reposted by Mintu Chandra
Journal of Cell Biology @jcb.org · 07/01/2026
The small #GTPase Rab1 is a master regulator of #Golgi traffic and #autophagy. van Vliet, Munro et al. @mrclmb.bsky.social performed a proteomic screen to identify novel Rab1 effectors, including a #dynein motor adaptor and cargo receptors for autophagy. rupress.org/jcb/article/... #Trafficking
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Janine Brunner @janinebrunner.bsky.social · 14/11/2025
MISO: microfluidic protein isolation enables single-particle cryo-EM structure determination from a single cell colony. Or from a single dish of HEK cell culture in the case of two membrane proteins. Out in Nature Methods now! lnkd.in/gpyBSceg Wonderful collaboration with the Efremov lab.
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Reposted by Mintu Chandra
Brett Collins @brettcollins.bsky.social · 11/11/2025
Beautiful new structure of the VPS13C lipid transfer protein from the Reinisch and De Camilli labs. @pdc-lab.bsky.social
biorxiv.org
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Reposted by Mintu Chandra
De Camilli Lab @pdc-lab.bsky.social · 29/09/2025
"Impaired hematopoiesis and embryonic lethality at midgestation of mice lacking both lipid transfer proteins VPS13A and VPS13C" out now in PLOS Biology journals.plos.org/plosbiology/...
journals.plos.org
Impaired hematopoiesis and embryonic lethality at midgestation of mice lacking both lipid transfer proteins VPS13A and VPS13C
VPS13A and VPS13C are bridge-like lipid transport proteins with distinct subcellular localization and function, and their absence is linked with chorea-acanthocytosis and Parkinson's disease, respecti...
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Reposted by Mintu Chandra
Cell Biology J-Club @cellclub.bsky.social · 17/09/2025
Version of Record Structural basis for mTORC1 activation on the lysosomal membrane www.nature.com/articles/s41...
nature.com
Structural basis for mTORC1 activation on the lysosomal membrane - Nature
Cryo-electron microscopy was used to study human mechanistic target of rapamycin complex 1 (mTORC1) activation on lysosomal membranes, showing progressive recruitment by RAG–Ragulator, RHEB and R...
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Ed Twomey @cryoet.bsky.social · 16/09/2025
🚨🧠🔬 A major breakthrough in molecular neuroscience: I am excited to share a new story from our lab, published in accelerated format today by @nature.com: "Delta-type glutamate receptors are ligand-gated ion channels" Read more here (free article link): rdcu.be/eGIKz
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Jeremy Baskin @jeremybaskin.bsky.social · 20/08/2025
Quite a week for #lipidtime: phenomenal study using bifunctional lipid probes to quantify intracellular lipid transport from @nadlerlab.bsky.social and colleagues is now out @nature.com! www.nature.com/articles/s41...
nature.com
Quantitative imaging of lipid transport in mammalian cells - Nature
Directional, non-vesicular lipid transport is responsible for fast, species-selective lipid sorting into organelle membranes.
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Reposted by Mintu Chandra
Katie Downes @dr-downes.bsky.social · 30/07/2025
Very excited to announce that my first, first author paper, is now on BioRxiv! In this paper we unambiguously show #COPII coated vesicles in unperturbed human cells for the very first time!! Make my day and check it out! www.biorxiv.org/content/10.1... #Cryo-ET #TeamTomo #Cryo-CLEM ❄️🔬❄️🔬❄️🔬❄️🔬
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Brett Collins @brettcollins.bsky.social · 30/07/2025
This was a fun paper to be involved in. Carlos identified many known and unknown proteins associated with endosomal membrane domains with really amazing proximity proteomics. @carlosantonplagaro.bsky.social @peterjcullen1.bsky.social
nature.com
Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation - Nature Communications
The endosomal retrieval subdomain organizes recycling of endocytosed proteins. Here, using proximity proteomics, the authors reveal that this recycling subdomain regulates switching of specific RAB GT...
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Reposted by Mintu Chandra
henrietteautzen.bsky.social @henrietteautzen.bsky.social · 28/07/2025
I am excited to share our latest preprint presenting the structure of human NHE6, a key endosomal Na⁺/H⁺ exchanger involved in Christianson syndrome. We bring together #cryo-EM, NMR, SAXS, lipidomics, and functional assays for an integrative analysis of NHE6 architecture, function, and regulation.
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Mintu Chandra @mintuju.bsky.social · 21/03/2025
Excellent work from the lab of Ben Engel.
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Reposted by Mintu Chandra
bioRxivpreprint @biorxivpreprint.bsky.social · 23/02/2025
Arrayed CRISPR/Cas9 Loss-Of-Function Screen in a Neuronal Model of Adaptor Protein Complex 4 Deficiency Identifies Modulators of ATG9A Trafficking www.biorxiv.org/content/10.1101/202…
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Reposted by Mintu Chandra
Jackson Lab @ Vanderbilt @lpjacksonlab.bsky.social · 14/02/2025
Excited to present our new story in Science Advances at #bps2025 meeting next week. Thanks to Vanderbilt CSB for featuring our work! www.vanderbilt.edu/csb/2025/02/...
vanderbilt.edu
Greater than the sum of its parts: the role of VARP-SNX27 binding in endosomal “supercomplex” formation
In cells, multi-subunit coat protein complexes are responsible for coordinating the transport of transmembrane proteins and lipid cargo between membranes. At the endosome, cargo trafficking is medi…
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Reposted by Mintu Chandra
Vanderbilt Center for Structural Biology @vanderbiltcsb.bsky.social · 14/02/2025
New work from the @lpjacksonlab.bsky.social uses a combination of biochemical, biophysical and computational modeling techniques to investigate endosomal trafficking players. Congrats to 1st author @mintuju.bsky.social! bit.ly/4hYry4o @vubasicsciences.bsky.social @vandybiomed.bsky.social
vanderbilt.edu
Greater than the sum of its parts: the role of VARP-SNX27 binding in endosomal “supercomplex” formation
In cells, multi-subunit coat protein complexes are responsible for coordinating the transport of transmembrane proteins and lipid cargo between membranes. At the endosome, cargo trafficking is medi…
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Mintu Chandra @mintuju.bsky.social · 13/02/2025
Thrilled to have my first-author publication in Science Advances, and grateful to my supervisor for sharing it on Bluesky! This marks a major milestone in our journey to unravel the complexities of endosomal protein interactions!
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Jackson Lab @ Vanderbilt @lpjacksonlab.bsky.social · 13/02/2025
The Jackson lab is thrilled to join Bluesky and find so many friends, scientists, and colleagues. It is an uncertain and frankly scary time for U.S. science, but today we are pausing to celebrate an exciting new paper in Science Advances: www.science.org/doi/10.1126/.... (Thread)
science.org
VARP binds SNX27 to promote endosomal supercomplex formation on membranes
VARP binds SNX27 to promote the assembly of the SNX27/Retromer/ESCPE-1 endosomal supercomplex on membranes.
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