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Printable Handouts
Navigable Slide Index
- Introduction
- Outline
- The adhesion type GPCR family
- Biological functions of aGPCRs
- Adhesion G protein coupled receptors (GPCRs)
- All aGPCRs have a GAIN domain
- The GAIN domain is a novel domain
- The cleaved peptide is hidden within GAIN domain
- GPS motif isn't an autonomously folded domain
- GAIN domain is evolutionarily conserved
- GAIN domain is widespread and conserved
- The GAIN domain is an autoproteolytic fold
- The two pieces do not separate (1)
- The two pieces do not separate (2)
- Hallmarks of the GAIN domain
- GAIN precedes the signaling membrane domain
- Working models for aGPCR activation
- Extracellular domains regulate receptor signaling
- Monobodies modulate GPR56 signaling
- Monobodies and the two complementary models
- Structures of aGPCR extracellular regions
- GPR56/ADGRG1 regulates brain development
- Predicted GPR56 domain structure
- The α5-GPR56 ECR complex structure
- PLL domain is deleted in GPR56 splice variant 4
- Splice variant 4 has higher basal activity
- The PLL domain has a highly-conserved patch
- PLL domain’s conserved patch & oligodendrocyte
- GPR56 function and its extracellular region
- Latrophilins/ADGRLs regulate synapse formation
- Trans-cellular adhesion GPCR/ligand complex
- Teneurins functions in embryogenesis
- 3.1 A cryo-EM structure of human teneurin-2
- TEN2 is highly resembles bacterial Tc toxins
- Alternative-splice dependent functions of teneurin-2
- Visualization of aGPCRs and cell-cell contacts
- Hormone binding domain of aGPCRs
- Drugs can be targeted to TM or extracellular region
- Acknowledgements
Topics Covered
- The history, biological functions and architecture of adhesion GPCRs
- The conserved GAIN domain
- Working models for adhesion GPCR activation
- The structures of adhesion GPCR extracellular regions and their ligands
- Similarity of adhesion GPCRs to hormone receptors
- Drugs might affect adhesion GPCRs via the extracellular regions or protein-protein interaction sites
Links
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Talk Citation
Araç, D. (2019, September 26). Structure and function of adhesion GPCRs and their ligands [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 21, 2024, from https://doi.org/10.69645/ZMFY1947.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Araç states there are no conflicts of interest.
Other Talks in the Series: G Protein-Coupled Receptors (GPCRs) Signaling in Health and Disease
Transcript
Please wait while the transcript is being prepared...
0:00
Hello, my name is Demet Arac,
and I'm an assistant professor at
the Department of Biochemistry and Molecular Biology at the University of Chicago.
My lab's primary focus is understanding the mechanisms of
adhesion GPCR action using structural and functional tools.
Today, I will be talking to you about
the structures and functions of adhesion GPCRs and their ligands.
0:30
The outline of this talk includes history,
biological function, and the architecture of adhesion GPCRs,
followed by the description of a conserved domain of adhesion GPCRs,
called the GAIN domain;
the working models for adhesion GPCR activation,
the structures of adhesion GPCR extracellular regions, and their ligands;
the similarity of adhesion GPCRs to hormone receptors,
and how adhesion GPCRs may be drugged.
1:07
The first adhesion GPCR was described in 1981,
and since then a total of 33 adhesion GPCRs were described in humans,
making adhesion GPCRs the second-largest GPCR family.
These genes are very large and complex genes,
and thus, they were often ignored by most studies.
As a result, adhesion GPCRs remains the
least studied and least understood family of GPCRs.
Initially, adhesion GPCRs were classified under the class B GPCRs.
In 2003, they were classified as a separate GPCR family,
and were named the adhesion GPCRs.