Raffaella De Pace
@depaceraffa.bsky.social
Staff Scientist Currently at NIH/NICHD, Bonifacino Lab Neurobiology-Cell Biology-Intracellular Trafficking. The views expressed in this account are mine alone.
Many thanks, @depaceraffa.bsky.social! I am deeply honored by this recognition and grateful to all who made it possible. 🙏
Raffaella De Pace@depaceraffa.bsky.social · 3mo agoCongratulations to @juanbonifacino.bsky.social at the NIH on his election to the American Academy of Arts and Sciences — one of the nation's most prestigious honorary societies — in recognition of his distinguished contributions to cellular and developmental biology! 🎉 www.amacad.org/new-members-...
Congratulations to @juanbonifacino.bsky.social at the NIH on his election to the American Academy of Arts and Sciences — one of the nation's most prestigious honorary societies — in recognition of his distinguished contributions to cellular and developmental biology! 🎉 www.amacad.org/new-members-...
New work from Niccolo Mencacci @feinberg.northwestern.edu et al., with contribution from @depaceraffa.bsky.social in our lab at the NIH, identifies pathogenic variants in BORCS5, encoding a subunit of the BORC complex, as a cause of a severe neurodevelopmental disorder. www.jci.org/articles/vie...
Take a look at our Research Highlight: Adriana Golding et al. www.nature.com/articles/s41... We highlight the work by Ghoochani et al., who generated an atlas of brain lysosomal proteins and identified SLC45A1-associated disease as a lysosomal disorder: www.cell.com/cell/fulltex...
🔥Excited to share our new paper! We describe patients from seven independent families carrying pathogenic BLOC1S1 variants, presenting with severe neurodevelopmental disorder. These variants disrupt BLOC-1/BORC complexes. Congrats to all co-authors! 👏 authors.elsevier.com/c/1mqGAgeXHm-E
Juan S. Bonifacino@juanbonifacino.bsky.social · 4mo agoNew from @depaceraffa.bsky.social from our lab #NICHD #NIH with Carlos Dominguez-Gonzalez, Adeline Vanderver @childrensphila.bsky.social et al.: pathogenic BLOC1S1 variants disrupt BLOC-1/BORC complexes in children with severe neurodevelopmental disorder authors.elsevier.com/c/1mqGAgeXHm-E
Latest preprint from our lab reports that the distinct pH of anterograde (less acidic) and retrograde (more acidic) lysosomal vesicles in the axon depends on assembly of the V1 and V0 domains of the vacuolar H+ ATPase, mediated by the metazoan RAVE complex www.biorxiv.org/content/10.6...
🚨🚨🚨 Please repost We are looking for postdocs to join our lab at NIH. Apply: www.nichd.nih.gov/research/atNICHD/Investigators/rocha/apply Learn more about training at NIH : www.training.nih.gov/research-tra...
Thank you, @mishtudey.bsky.social and @cp-cellchembiol.bsky.social for featuring this interview with @depaceraffa.bsky.social and Chad Williamson in connection to our article on BLOC-1 and BORC dlvr.it/TN9mpn
Cell Chemical Biology@cp-cellchembiol.bsky.social · 11mo agoMeet the authors: Raffaella De Pace, Chad Williamson, and Juan Bonifacino http://dlvr.it/TN9cVw
👉 New publication ahead of print from our lab: tinyurl.com/ye7pntte We show that the protein SPG21, mutated in hereditary spastic paraplegia 21, localizes to endolysosomes via RAB7A, where it promotes mTORC1-dependent TFEB phosphorylation, reducing expression of a subset of TFEB regulated genes
New from @depaceraffa.bsky.social from our lab #NICHD #NIH in collaboration with Adeline Vanderver @childrensphila.bsky.social and colleagues reporting mutations in the BLOC1S1 subunit of the BLOC-1 and BORC complexes in children with a neurodevelopmental disorder www.medrxiv.org/content/10.1...
Happy to share an exciting study from Yihong Ye’s lab at NIH, with a minor contribution from our lab: ceroid lipofuscinosis-4 (CLN4)-linked DNAJC5 mutations cause lysosomal damage as a driver of neurodegeneration in iPSC-derived neurons. CHIP safeguards lysosomes via microautophagy 👉 rdcu.be/eChof
CHIP protects lysosomes from CLN4 mutant-induced membrane damage
Nature Cell Biology - Lee et al. use an aggregation-prone CLN4 mutant that causes lysosomal damage in neurons and show that in non-neurons, the ubiquitin ligase CHIP prevents CLN4-dependent...
rdcu.be
Excited to share our new review with @depaceraffa.bsky.social, @saikat2025.bsky.social, and Chad Williamson on the BLOC-1 and BORC complexes—key regulators of endolysosomal processes and linked to several genetic diseases. #NIH #Lysosomes #RareDiseases authors.elsevier.com/a/1lg4i8jWWJ...
🚨 Exciting postdoc opportunity in @juanbonifacino.bsky.social lab!! If you have a passion for protein trafficking and neurodevelopmental disorders, and want to join a dynamic and collaborative team consider applying! Positions will be available starting in October.🍁🍂
Juan S. Bonifacino@juanbonifacino.bsky.social · last yr.Our lab at the NIH (Bethesda, MD) is looking for postdoctoral fellows to join our team studying the molecular mechanisms of protein trafficking and their links to neurodevelopmental disorders starting on or after 10-1-2025. Send your application to juan.bonifacino@nih.gov. Please share and repost!
I’m so excited to organize the #Lysosomes Subgroup at @ASCBiology 2024 meeting on Sunday, Dec. 15 at 3:15pm, Room 33B. Lysosomes naturally lend themselves to puns. So…Don’t be 𝒃𝒂𝒔𝒊𝒄. Join us for fresh, 𝒄𝒖𝒕𝒕𝒊𝒏𝒈-edge talks and puntastic times. It will 𝒆𝒂𝒕 𝒂𝒕 𝒚𝒐𝒖 if you miss it.
This post is about a commentary that I wrote with Xin Yong about recognition of cargo vesicles by tethering factors involved in endosomes to TGN retrograde transport.
Science News@scinews.bsky.social · 2y agoSelective cargo recognition by vesicle tethering factors Open Access doi.org/10.59717/j.x...
Kudos to authors Morié Ishida, Adriana Golding, @TalKerenKaplan @NICHD_NIH and our collaborators Tamas Balla @NICHD_NIH and Yan Li @NIH_NINDS! Great teamwork!
Excited to share our latest findings on how the phosphoinositide PI4P pool at the trans-Golgi network (TGN) is regulated through a SYS1-ARFRP1-ARL5-ARMH3-PI4KB pathway, in which ARMH3 (also known as C10orf76) acts as an ARL5 effector to activate PI4KB. rdcu.be/d1dZ2
Reposting @yousufakhan.bsky.social reference to a preprint demonstrating that programmed ribosomal frameshifting generates a PLEKHM2 proteoform that behaves as a constitutively active adaptor for ARL8-dependent coupling of lysosomes to kinesin-1, with collaboration from our lab tinyurl.com/mtrkzdrm
Programmed ribosomal frameshifting during PLEKHM2 mRNA decoding generates a constitutively active mediator of kinesin-1-dependent lysosome transport
Programmed ribosomal frameshifting is a translational recoding phenomenon in which a proportion of ribosomes are stimulated to slip backwards or forwards on an mRNA1, rephasing the ribosome relative t...
tinyurl.com
Yousuf A. Khan@yousufakhan.bsky.social · 2y ago2) #RNA elements can dynamically recode the genome: they force the ribosome to change its reading frame dynamically. Viruses employ this routinely (HIV, SARS-CoV2) but this mechanism in humans had been controversial until we found the first human hit in PLKEHM2 (www.biorxiv.org/content/10.1...) 2/3
