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Undergraduate research assistants and Graduate students candidates who are interested in carrying out research rotations in the following areas are especially encouraged to contact the group by emailing Dr. Gregory Tall at gregtall@umich.edu with a cover letter addressing your specific interest:
Undergraduate research assistants and Graduate students candidates who are interested in carrying out research rotations in the following areas are especially encouraged to contact the group by emailing Dr. Gregory Tall at gregtall@umich.edu with a cover letter addressing your specific interest:
- G protein-coupled receptor (GPCR) signaling
- Translational hematology
- Mechanism of Adhesion-GPCR Action
- Heterotrimeric G protein Biosynthesis
- G protein somatic mutation diseases
- Alternative Functions of Ric-8 proteins
Heterotrimeric G protein Biosynthesis
Heterotrimeric G protein Biosynthesis
Ric-8 proteins fold newly made G protein α subunits. The G protein heterotrimer then assembles and transits to the plasma membrane residence. Ric-8A and Ric-8B are required to collectively maintain normal levels of all G proteins.
Ric-8 proteins fold newly made G protein α subunits. The G protein heterotrimer then assembles and transits to the plasma membrane residence. Ric-8A and Ric-8B are required to collectively maintain normal levels of all G proteins.
Current Directions:
Current Directions:
- Regulation of Ric-8 activity to tune total cellular G protein signaling.
- Development of Ric-8 modulatory probe compounds.
- Ric-8 based technology to purify all G protein α subunits.
Mechanism of Adhesion GPCR Action
Mechanism of Adhesion GPCR Action
Adhesion GPCRs comprise 10% of the non-olfactory GPCRome and have diverse roles in tissue development. The receptors undergo self-cleavage to become two fragment receptors. The large ectodomains of the receptor class conceal an element that becomes the 7TM domain tethered peptide agonist upon fragment dissociation.
Adhesion GPCRs comprise 10% of the non-olfactory GPCRome and have diverse roles in tissue development. The receptors undergo self-cleavage to become two fragment receptors. The large ectodomains of the receptor class conceal an element that becomes the 7TM domain tethered peptide agonist upon fragment dissociation.
Current Directions:
Current Directions:
- Understanding physiologic mechanisms of adhesion GPCR activation and tethered agonism.
- Development of first-in-class adhesion GPCR small molecule modulators through high-throughput screening.
G protein somatic mutation diseases
G protein somatic mutation diseases
Gαq activating mutations (GTPase defective) cause disease including uveal melanoma, skin lesions such as blue nevi, and Sturge-Weber syndrome.
Gαq activating mutations (GTPase defective) cause disease including uveal melanoma, skin lesions such as blue nevi, and Sturge-Weber syndrome.
Current Directions:
Current Directions:
Suppression of Gαq oncoprotein action by Ric-8A targeting or Gq pathway hyperstimulus.
Suppression of Gαq oncoprotein action by Ric-8A targeting or Gq pathway hyperstimulus.
Alternative Functions of Ric-8 proteins
Alternative Functions of Ric-8 proteins
We originally described the activity of Ric-8 proteins as Gα subunit guanine nucleotide exchange factors. There is no clear evidence to date that Ric-8 activates G proteins in cells for the same purpose that GPCRs do: to evoke signaling stimulus. However, Ric-8 proteins reside on subcellular structures, including the mitotic spindle and cellular membranes, suggesting additional functionality beyond solely acting as cytosolic, Gα subunit biosynthetic chaperones.
We originally described the activity of Ric-8 proteins as Gα subunit guanine nucleotide exchange factors. There is no clear evidence to date that Ric-8 activates G proteins in cells for the same purpose that GPCRs do: to evoke signaling stimulus. However, Ric-8 proteins reside on subcellular structures, including the mitotic spindle and cellular membranes, suggesting additional functionality beyond solely acting as cytosolic, Gα subunit biosynthetic chaperones.
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