Cycles of autoubiquitination and deubiquitination regulate the ERAD ubiquitin ligase Hrd1.
Peterson BG, Glaser ML, Rapoport TA, Baldridge RD
eLife, 2019, 8
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Everyone has tried to fit pieces of something they've broken back together to make it work again. This is one approach we use in our everyday science
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Liposomes!
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Toothless... the workhorse of our lab...
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Beautiful.
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Proteoliposomes float to the top!
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This is home for our yeasty-beasties
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Our model organism of choice.
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Proteoliposomes imaged with a single-molecule setup
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mScarlet-I purification
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View from the lab
Protein Quality Control at Cellular Membranes
Our lab focuses on the mechanism by which cells recognize and dispose of misfolded proteins within their organelles. These processes are remarkably conserved, and we use Saccharomyces cerevisiae as a model system, because of its simplicity relative to "higher" eukaryotes. Our Research »Selected Publications
View all »Autoubiquitination of the Hrd1 ligase triggers protein retrotranslocation in ERAD.
Baldridge RD, Rapoport TA
Cell, 2016, 166 (2), 394-407
View on PubMed »Two-gate mechanism for phospholipid selection and transport by type IV P-type ATPases.
Baldridge RD, Graham TR
Proceedings of the National Academy of Sciences of the United States of America, 2013, 110 (5), E358-67
View on PubMed »Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases.
Baldridge RD, Graham TR
Proceedings of the National Academy of Sciences of the United States of America, 2012, 109 (6), E290-8
View on PubMed »Latest News
View all »Our first publication is out! Congratulations to Brian!
https://elifesciences.org/articles/50903
PFD symposium takeover… Brian, Devon, Rachel, and Jiwon
Congratulations to Brian, Rachel, and Jiwon for winning their categories at the poster session!
Congratulations to Brian for his NSF GRFP award, well deserved!
His CV is building up quickly!
The results for the 2019 #NSF Graduate Research Fellowship Program competition have been announced! #NSFGRFP https://t.co/KqhhCUA3Uj
— NSF GRFP (@NSFGRFP) April 9, 2019
We are interested in motivated scientists and scientists-in-training at all levels!
Please contact Ryan if you are interested in working with us in any capacity to see what options are available.
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