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Nuclear G-Protein Coupled Receptors: Methods and Protocols is a
compilation of a number of conceptual and methodological aspects
important for the validation and characterization of intacrine
signaling systems. To date, the best-characterized intracrine
signaling system is that of angiotensin II (Ang II), covered in
depth in various chapters. Methodology to study the subcellular
localization and function of GPCRs and other signaling systems is
provided, as well as numerous chapters focusing on methods designed
to understand signaling mediated by nuclear and other internal
GPCRs. Methods are also described to study the formation of second
messengers such as cAMP and to study the trafficking of receptors
from the cell surface. Written in the successful Methods in
Molecular Biology series format, chapters include introductions to
their respective topics, lists of the necessary materials and
reagents, step-by-step, readily reproducible protocols, and notes
on troubleshooting and avoiding known pitfalls. Authoritative and
easily accessible, Nuclear G-Protein Coupled Receptors: Methods and
Protocols seeks to serve both professionals and novices with
state-of-the-art approaches to characterize what is becoming a
common theme in cellular signaling.
Main Question: G protein coupled receptors are involved in highly
efficient and specific activation of signalling pathways. How do
GPCR signalling complexes get assembled to generate such
specificity? In order to answer this question, we need to
understand how receptors and their signalling partners are
synthesized, folded and quality-controlled in order to generate
functional proteins. Then, we need to understand how each partner
of the signalling complex is selected to join a complex, and what
makes this assembly possible. GPCRs are known to be able to
function as oligomers, what drives the assembly into oligomers and
what will be the effects of such organization on specificity and
efficacy of signal transduction. Once the receptor complexes are
assembled, they need to reach different locations in the cell; what
drives and controls the trafficking of GPCR signalling complexes.
Finally, defects in synthesis, maturation or trafficking can alter
functionality of GPCRs signalling complexes; how can we manipulate
the system to make it function normally again? Pharmacological
chaperones may just be part of the answer to this question.
Nuclear G-Protein Coupled Receptors: Methods and Protocols is a
compilation of a number of conceptual and methodological aspects
important for the validation and characterization of intacrine
signaling systems. To date, the best-characterized intracrine
signaling system is that of angiotensin II (Ang II), covered in
depth in various chapters. Methodology to study the subcellular
localization and function of GPCRs and other signaling systems is
provided, as well as numerous chapters focusing on methods designed
to understand signaling mediated by nuclear and other internal
GPCRs. Methods are also described to study the formation of second
messengers such as cAMP and to study the trafficking of receptors
from the cell surface. Written in the successful Methods in
Molecular Biology series format, chapters include introductions to
their respective topics, lists of the necessary materials and
reagents, step-by-step, readily reproducible protocols, and notes
on troubleshooting and avoiding known pitfalls. Authoritative and
easily accessible, Nuclear G-Protein Coupled Receptors: Methods and
Protocols seeks to serve both professionals and novices with
state-of-the-art approaches to characterize what is becoming a
common theme in cellular signaling.
Main Question: G protein coupled receptors are involved in highly
efficient and specific activation of signalling pathways. How do
GPCR signalling complexes get assembled to generate such
specificity? In order to answer this question, we need to
understand how receptors and their signalling partners are
synthesized, folded and quality-controlled in order to generate
functional proteins. Then, we need to understand how each partner
of the signalling complex is selected to join a complex, and what
makes this assembly possible. GPCRs are known to be able to
function as oligomers, what drives the assembly into oligomers and
what will be the effects of such organization on specificity and
efficacy of signal transduction. Once the receptor complexes are
assembled, they need to reach different locations in the cell; what
drives and controls the trafficking of GPCR signalling complexes.
Finally, defects in synthesis, maturation or trafficking can alter
functionality of GPCRs signalling complexes; how can we manipulate
the system to make it function normally again? Pharmacological
chaperones may just be part of the answer to this question.
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