Related Experiment Video

Updated: Jul 4, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
10:50

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

pVHL: a multipurpose adaptor protein

Ian J Frew1, Wilhelm Krek

  • 1Institute of Cell Biology, Eidgenössische Technische Hochschule Zurich, 8093 Zurich, Switzerland.

Science Signaling
|June 19, 2008
PubMed

Insights

Mutations in the von Hippel-Lindau (VHL) gene are linked to various tumors. The VHL protein (pVHL) acts as an adaptor, regulating gene expression and cellular processes, with its dysfunction contributing to tumor formation.

Area of Science:

  • Molecular Biology
  • Oncology
  • Genetics

Background:

  • Mutations in the von Hippel-Lindau (VHL) tumor suppressor gene are implicated in inherited and sporadic tumors.
  • The VHL protein (pVHL) lacks enzymatic activity but is crucial for cellular function through protein interactions.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying pVHL's tumor suppressor functions.
  • To understand how pVHL's interactions with multiprotein complexes influence cellular processes and contribute to tumorigenesis.

Main Methods:

  • Analysis of pVHL-containing multiprotein complexes.
  • Investigation of pVHL's role in gene expression, extracellular matrix assembly, and microtubule-based processes.

Main Results:

  • pVHL functions as a versatile adaptor protein.
  • pVHL links target proteins to enzymatic activities, regulating diverse cellular functions.
  • Dysregulation of pVHL's molecular activities is associated with tumor formation.

Conclusions:

  • pVHL plays a multifaceted role in maintaining cellular homeostasis and preventing tumor development.
  • Understanding pVHL's complex interactions provides insights into VHL-associated tumor pathogenesis.
  • Targeting pVHL-mediated pathways may offer therapeutic strategies for VHL-related cancers.

More Related Videos

In vivo and in vitro Studies of Adaptor-clathrin Interaction17:14

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

Utilizing the Antigen Capsid-Incorporation Strategy for the Development of Adenovirus Serotype 5-Vectored Vaccine Approaches13:36

Utilizing the Antigen Capsid-Incorporation Strategy for the Development of Adenovirus Serotype 5-Vectored Vaccine Approaches

Published on: May 6, 2015

Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
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...
The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...