Joachim Seemann
University of Texas Southwestern Medical Center, TX·Biology
Every cell has to package and ship proteins and fats, such as receptors, hormones and growth factors, to the right places. The Golgi apparatus is the cell's central sorting and processing station for this job.
- Fields
Biology
Biochemistry
- Topics
Golgi apparatus
Golgi ribbon
golgins
- Grants
- 1 known grant, through Jun 2030
What they work on
- Identify and characterize the RNA–golgin scaffolds that link Golgi stacks into a ribbon, focusing on how the golgin GM130 recruits RNA to Golgi membranes, using biochemical and microscopy approaches.
- Define how the organization of RNA–golgin condensates, droplet-like clusters formed by phase separation, supports Golgi processing and sorting of proteins at the molecular level.
- Determine how the RNA–golgin scaffold is regulated so that the Golgi ribbon can unlink under stress and during mitosis, when Golgi membranes are divided between daughter cells.
More about the research
In mammalian cells, many Golgi stacks are joined side by side into one continuous ribbon. When this ribbon breaks apart or stops working, it is linked to diseases such as metastatic cancer, neurodegenerative disorders and muscular dystrophies. Yet it is still unclear how the ribbon is built and held together.
Why it matters
Golgi fragmentation is common in human diseases including metastatic cancer, neurodegeneration and muscular dystrophy. Learning how RNA and golgins hold the Golgi ribbon together could reveal how these diseases disrupt cells' protein-shipping system. It could also show more broadly how cells use phase separation to organize their compartments.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Julia Von Blume
Yale University, CT·Biology
Define the molecular requirements for chromogranins and Cab45 to form liquid condensates by liquid-liquid phase separation, using reconstituted systems that mimic the chemical environment inside the trans-Golgi Network.
Danfeng Cai
Johns Hopkins University, MD·Biochemistry
Determine how RNA binding through RNA-recognition motifs, together with coiled-coil domains, drives the NONO-TFE3 and SFPQ-TFE3 fusion oncoproteins to form condensates in the nucleus.
Bruce Armitage
Carnegie Mellon University, PA·Chemistry
Design fluorescent peptide nucleic acid (PNA) probes that bind unmodified C9orf72 repeat RNAs, so these RNAs can be seen in biomolecular condensates by microscopy.
The school
University of Texas Southwestern Medical Center: 40 labs on PI Pages, $869M a year on research, 86 research doctorates a year.
Reach out
A start for your email. Fill in the brackets.