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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Docking proteins.

Tilman Brummer1, Carsten Schmitz-Peiffer, Roger J Daly

  • 1Centre for Biological Systems Analysis (ZBSA), Albert-Ludwigs-University of Freiburg, Freiburg, Germany.

The FEBS Journal
|October 2, 2010
PubMed
Summary
This summary is machine-generated.

Docking proteins are noncatalytic intracellular signaling molecules. This review explores the structure, function, and regulation of key docking protein families involved in cellular processes.

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Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Biochemistry

Background:

  • Docking proteins are crucial intracellular, noncatalytic signaling molecules.
  • They function downstream of receptor tyrosine kinases, influencing diverse physiological and pathological processes.
  • Key families include Growth Factor Receptor Bound 2-Associated Binder/Daughter of Sevenless (GAB/Dose), Insulin Receptor Substrate (IRS), Fibroblast Growth Factor Receptor Substrate 2 (FRS2), and Downstream of Tyrosine Kinases (DOK) proteins.

Purpose of the Study:

  • To provide a comprehensive overview of docking proteins.
  • To focus on the structure, function, and regulation of major docking protein families.
  • To highlight their role in signal transduction pathways.

Main Methods:

  • Literature review and synthesis of existing research.
  • Analysis of structural, functional, and regulatory data.
  • Comparative examination of different docking protein families.

Main Results:

  • Docking proteins act as scaffolds, integrating signals from various receptors.
  • Their structure dictates their function and interaction with signaling partners.
  • Regulation occurs through post-translational modifications and protein-protein interactions.

Conclusions:

  • Docking proteins are essential regulators of signal transduction.
  • Understanding their structure-function relationships is key to deciphering complex cellular processes.
  • Dysregulation of docking proteins is implicated in various diseases, offering therapeutic targets.