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Related Concept Videos

Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical, 7TM, or...

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Related Experiment Video

Updated: May 11, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Seven-transmembrane receptors.

Kristen L Pierce1, Richard T Premont, Robert J Lefkowitz

  • 1The Howard Hughes Medical Institute and the Department of Medicine, Box 3821, Duke University Medical Center, Durham, North Carolina 27710, USA.

Nature Reviews. Molecular Cell Biology
|September 5, 2002
PubMed
Summary
This summary is machine-generated.

Seven-transmembrane receptors are key drug targets, but current models of G-protein signaling don't fully explain their diverse biological functions. Further research is needed to understand these complex membrane receptors.

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Last Updated: May 11, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Published on: May 26, 2011

Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
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Published on: June 9, 2017

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Seven-transmembrane receptors (7TMRs) represent the largest and most versatile family of membrane receptors.
  • These receptors are the primary targets for a vast majority of therapeutic drugs.
  • Existing models of G-protein coupling and second-messenger activation inadequately explain the full spectrum of 7TMR functions.

Purpose of the Study:

  • To highlight the limitations of current models in explaining the diverse biological actions of seven-transmembrane receptors.
  • To emphasize the need for updated or novel mechanistic insights into 7TMR signaling pathways.
  • To underscore the importance of understanding 7TMRs for drug development.

Main Methods:

  • Review of existing literature on seven-transmembrane receptor signaling.
  • Analysis of classical G-protein coupling and second-messenger activation pathways.
  • Identification of discrepancies between established models and observed biological actions.

Main Results:

  • Classical G-protein coupling models fail to account for the full range of seven-transmembrane receptor activities.
  • Second-messenger generation pathways do not fully explain the diverse cellular responses mediated by 7TMRs.
  • Significant gaps exist in the current understanding of seven-transmembrane receptor signaling mechanisms.

Conclusions:

  • The established models of seven-transmembrane receptor signaling are incomplete.
  • A deeper understanding of seven-transmembrane receptor biology is crucial for advancing therapeutic strategies.
  • Future research should focus on uncovering novel signaling mechanisms employed by these critical membrane proteins.