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Printable Handouts
Navigable Slide Index
- Introduction
- Arrestins
- Homologous desensitization
- Two branches of GPCR signaling
- How does arrestin know when to bind?
- Sequential multi-site binding
- Conformational change during arrestin binding
- Number of receptor molecules arrestin binds
- Arrestin: GPCR binding ratio
- Arrestin-1 self-association
- Only arrestin monomer binds rhodopsin
- Nanodiscs
- Monomeric receptor binds arrestin
- Arrestin-1 rhodopsin complex
- DEER distances in the rhodopsin–arrestin complex
- Refined rhodopsin-arrestin complex
- The polar core in arrestin-1
- Effects of defects in rhodopsin phosphorylation
- Enhanced arrestin-1-3A
- Finger loop plays key role in receptor binding
- Arrestin chimeras
- Residues that determine receptor preference
- The effects of several mutations are additive
- Where do GPCRs and other partners bind?
- Role of arrestin in GPCR internalization
- Arrestin switches
- comparison of ERK1/2 and JNK3 activation
- Arrestin-3-KNC binding to JNK3
- Suppressing JNK signaling by a silent scaffold
- Arrestin-3 derived mini-scaffold activates JNK3
- Conveyor belt model
- Summary
Topics Covered
- Arrestins
- Arrestin-GPCR binding and signaling
- Nanodiscs
- Arrestin-rhodopsin binding
- Arrestin protein biochemistry
- Physiological effects of mutations
Links
Series:
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Talk Citation
Gurevich, V.V. (2021, August 29). Biology and structure of arrestin proteins [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 3, 2024, from https://doi.org/10.69645/SITO8742.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Vsevolod V. Gurevich has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
Other Talks in the Series: G Protein-Coupled Receptors (GPCRs) Signaling in Health and Disease
Transcript
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0:00
My name is Seva Gurevich, I'm from Vanderbilt University in Nashville, Tennessee.
We will discuss the structure and biological functions of arrestin proteins.
0:12
Arrestins were first discovered as proteins that bind
active phosphorylated G protein-coupled receptors (GPCRs for short).
All animals have hundreds of different GPCR sub-types, that respond to a variety of stimuli.
Structurally, GPCR activators range from photons of light, ions,
small molecules, to peptides and to large proteins.
GPCRs activate heterotrimeric G proteins,
that's why they are called G protein-coupled receptors.
Activated G proteins, in their turn, activate a variety of intracellular effects.
Here is the structure of a prototypical GPCR, rhodopsin,
which mostly consists of the conserved GPCR core, that includes
seven transmembrane helices forming a twisted bundle.
The first discovered function of arrestins was
their role in homologous desensitization of GPCRs,
that is, the loss of sensitivity of the activated receptor.
Active receptors sequentially activate many G protein molecules.
The active receptor is phosphorylated by GRKs (GPCR kinases),
arrestins then bind active phosphorylated receptors,
blocking their coupling to G proteins.
1:26
Receptor-bound arrestins bind clathrin and clathrin adaptor AP2,
facilitating receptor internalization, and interact with
a variety of effectors initiating certain branches of signaling.