LLPS Mini-symposium
Phase separation has emerged as a crucial mechanism for organizing biochemical reactions in cells, impacting from basic biological functions to diseases. In this mini-symposium, we are delighted to welcome Dr. Tanja Mittag, a leading pioneer in the field of biomolecular condensates. Her research spans fundamental biophysical properties, cellular mechanisms, and their implications in cancers and neurodegenerative diseases. Dr. Mittag will share her latest findings and insights into the forefront of this exciting field.
In addition, we are pleased to present nine outstanding researchers from Taiwan, each contributing unique perspectives and advancing our understanding of phase separation and biomolecular condensates in various biological contexts. Below is the schedule and list of talks for the symposium. Full abstracts will be available on the symposium date, and additional information about each speaker can be found through the hyperlinks to their names.
We hope this symposium will foster stimulating discussions and collaborations, offering new insights into the dynamic world of phase separation and its impact on biological functions and diseases.
Symposium Agenda
- 10:00~10:10 Opening
- 10:10~11:00 Tanja Mittag: Phase separation and emergent properties of condensates
- 11:00~11:30 Ruey-Hwa Chen: PAICS ubiquitination recruits UBAP2 to trigger phase separation for purinosome assembly
- 11:30~12:00 Won-Jing Wang: Phase separation of TTBK2 and CEP164 is necessary for ciliogenesis
- 12:00~12:30 Woan-Yuh Tarn: Phase separation of ribonucleoprotein complexes for DNA damage repair
- 12:30~2:00 Lunch
- 2:00~2:30 Su Hao Lo: Development of biomolecular condensates at focal adhesions
- 2:30~3:00 Kuo-Chiang Hsia: HSET-dependent transport and adhesion contribute to the clustering of acentriolar centrosomes in cancer cells
- 3:00~3:30 Chun-Wei Lin: Crowding-driven phase transition on the membrane
- 3:30~3:45 Short Break
- 3:45~4:15 Jie-rong Huang: The evolution of intrinsically disordered regions in vertebrate galectins for phase separation
- 4:15~4:45 Joseph Jen-Tse Huang: Condensation and aggregation of nucleic acid-binding proteins in amyotrophic lateral sclerosis
- 4:45~5:15 Rita Pei-Yeh Chen: Phosphorylation-induced self-coacervation versus RNA-assisted complex coacervation of Tau proteins
- 5:15~6:00 Discussion
- 6:00~ Dinner
Selected publications from Tanja Mittag's lab
- Farag M, Borcherds WM, Bremer A, Mittag T*, Pappu RV*. Phase separation of protein mixtures is driven by the interplay of homotypic and heterotypic interactions. Nat Commun;14(1):5527, 2023.
- Cuneo MJ, O'Flynn BG, Lo, Y-H, Sabri N, Mittag T*. Higher-order SPOP assembly reveals a basis for cancer mutant dysregulation. Mol Cell, 2023.
- Bremer A, Farag M, Borcherds WM, Peran I, Martin EW, Pappu RV*, Mittag T*. Deciphering how naturally occurring sequence features impact the phase behaviors of disordered prion-like domains. Nat Chemistry 13: 196-207, 2022.
- Martin EW, Harmon TS, Hopkins JB, Chakravarthy S, Incicco J, Schuck P, Soranno A, Mittag T*. A multi-step nucleation process determines the kinetics of prion-like domain phase separation. Nat Commun. 12(1):4513, 2021.
- Martin EW, Thomasen FE, Milkovic NM, Cuneo MJ, Grace CR, Nourse A, Lindorff-Larsen K, Mittag T*. Interplay of folded domains and the disordered low-complexity domain in mediating hnRNPA1 phase separation. Nucleic Acids Res 49(5): 2931-2945, 2021.
- Martin EW, Holehouse AS, Peran I, Farag M, Incicco JJ, Bremer A, Grace CR, Soranno A, Pappu RV*, Mittag T*. Valence and patterning of aromatic residues determine the phase behavior of disordered prion-like domains. Science 367(6478):694-699, 2020.
- Schmit JD, Bouchard JJ, Martin EW, Mittag T*. Protein network structure enables switching between liquid and gel states. JACS 142(2):874-883, 2020.
- Bouchard JJ, Otero JH, Scott DC, Szulc EM, Martin EW, Sabri N, Granata D, Marzahn MR, Lindorff-Larsen K, Salvatella X, Schulman BA, Mittag T*. Cancer mutations of the tumor suppressor SPOP disrupt the formation of active, phase-separated compartments. Mol Cell 72:19-36, 2018.
- Martin EW, Holehouse A, Grace CR, Hughes A, Pappu RV, Mittag T*. Sequence determinants of the conformational properties of an intrinsically disordered protein prior to and upon multisite phosphorylation. JACS 138(47):15323-15335, 2016.
- Molliex A, Temirov J, Lee J, Coughlin M, Kanagaraj AP, Kim HJ, Mittag T*, Taylor JP*. Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization. Cell 163(1): 123-33, 2015.