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Related Concept Videos

Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
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...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or 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...

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Related Experiment Video

Updated: Jun 25, 2026

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SRBC/cavin-3 is a caveolin adapter protein that regulates caveolae function.

Kerrie-Ann McMahon1, Hubert Zajicek, Wei-Ping Li

  • 1Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9039, USA.

The EMBO Journal
|March 6, 2009
PubMed
Summary

SRBC acts as a crucial adapter molecule, binding to caveolin and facilitating intracellular transport of caveolae (cavicles). Its absence impairs cavicle movement, highlighting its role in regulating caveolae function.

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The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins
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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
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The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins
09:22

The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins

Published on: December 13, 2013

Area of Science:

  • Cell biology
  • Molecular and structural biology

Background:

  • Caveolae are essential membrane domains in most cells.
  • Caveolin is a key protein defining caveolae, but its function remains unclear.
  • Adapter molecules may be recruited to caveolae by caveolin, similar to clathrin in coated pits.

Purpose of the Study:

  • To characterize SRBC as a potential caveolin adapter molecule.
  • To investigate the role of SRBC in caveolae formation and intracellular transport.

Main Methods:

  • Co-immunoprecipitation assays to detect protein interactions.
  • Localization studies using microscopy.
  • Functional assays assessing cavicle traffic.

Main Results:

  • SRBC binds to PKCdelta and co-immunoprecipitates with caveolin-1.
  • A leucine zipper domain in SRBC is critical for caveolin binding and localization to caveolae.
  • SRBC remains associated with caveolin during cavicle budding and transport.
  • Absence of SRBC significantly impairs intracellular cavicle traffic.

Conclusions:

  • SRBC functions as a caveolin adapter molecule, crucial for regulating caveolae function.
  • SRBC, PTRF, and SDPR are identified as caveolin adapter proteins involved in caveolae dynamics.