Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Catenins

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...

Assembly of Signaling Complexes

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,...

Protein Complexes with Interchangeable Parts

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 Parts

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

An allosteric inhibitor of protein arginine methyltransferase 3.

Structure (London, England : 1993)·2012

Same author

A distinct replication fork protection pathway connects Fanconi anemia tumor suppressors to RAD51-BRCA1/2.

Cancer cell·2012

Same author

Cell intrinsic role of COX-2 in pancreatic cancer development.

Molecular cancer therapeutics·2012

Same author

Loss of the androgen receptor cofactor p44/WDR77 induces astrogliosis.

Molecular and cellular biology·2012

Same author

JNK and PTEN cooperatively control the development of invasive adenocarcinoma of the prostate.

Proceedings of the National Academy of Sciences of the United States of America·2012

Same author

Incidence of invasive squamous cell carcinomas in biopsy-proven squamous cell carcinomas in situ sent for Mohs micrographic surgery.

Dermatologic surgery : official publication for American Society for Dermatologic Surgery [et al.]·2012

Same journal

Association with serotonin transporter enables the phosphorylation of insulin receptor in placenta.

Current topics in biochemical research·2024

Same journal

Brain ethanol metabolism and mitochondria.

Current topics in biochemical research·2023

Same journal

The role of MiT/TFE family members in autophagy regulation.

Current topics in biochemical research·2022

Same journal

β-caryophyllene enhances the transcriptional upregulation of cholesterol biosynthesis in breast cancer cells.

Current topics in biochemical research·2021

Same journal

Biochemical and histopathological evaluation of Al<sub>2</sub>O<sub>3</sub> nanomaterials in kidney of Wistar rats.

Current topics in biochemical research·2019

Same journal

Preserved hydride transfer mechanism in evolutionarily divergent thymidylate synthases.

Current topics in biochemical research·2016

See all related articles

Search research articles

Related Experiment Video

Updated: May 27, 2026

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

PTEN-Associated Complexes: An Overview.

Sherly Mosessian¹, Hong Wu

¹Department of Molecular and Medical Pharmacology, UCLA.

Current Topics in Biochemical Research

|November 15, 2011

Summary

This summary is machine-generated.

PTEN, a key tumor suppressor, forms complexes with other proteins. Understanding these PTEN complexes is crucial for deciphering its roles in cell growth, survival, and development.

More Related Videos

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Related Experiment Videos

Last Updated: May 27, 2026

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Area of Science:

Molecular biology
Cell biology
Biochemistry

Background:

PTEN (Phosphatase and tensin homolog) is a crucial tumor suppressor.
It functions as a lipid phosphatase, counteracting the PI3K/Akt pathway.
PTEN plays vital roles in embryonic development, cell proliferation, survival, and stem cell maintenance.

Purpose of the Study:

To review the known PTEN complex components.
To discuss the biological functions of these PTEN complexes.
To explore the regulation of PTEN complex formation and function.

Main Methods:

Literature review of recent studies identifying PTEN-interacting proteins.
Analysis of PTEN's subcellular localization and complex formation.
Integration of data on PTEN complex functions and regulation.

Main Results:

PTEN forms high molecular weight complexes in various subcellular locations.
These complexes involve diverse proteins that modulate PTEN's phosphatase activity and cellular roles.
Identification of PTEN complex components provides insights into its multifaceted functions.

Conclusions:

PTEN complex formation is integral to its tumor-suppressive activity.
Understanding PTEN complexes is essential for elucidating its roles in development and disease.
Further research into PTEN complex regulation may reveal therapeutic targets.