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...

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

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.

Beautiful new structure of the VPS13C lipid transfer protein from the Reinisch and De Camilli labs. @pdc-lab.bsky.social

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...

"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/...

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...

Version of Record
Structural basis for mTORC1 activation on the lysosomal membrane
www.nature.com/articles/s41...

🚨🧠🔬 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

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.

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...

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 ❄️🔬❄️🔬❄️🔬❄️🔬

Many congratulations Brett and team. Exciting findings

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...

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

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.

Congratulations Kevin and Brett! Great work

Excellent work from the lab of Ben Engel.

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/10.1101/2025.02....

Thank you!

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…

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/...

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…

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

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!

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.

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)