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...

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,...

Assembly of Complex Microtubule Structures

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.

Formation of Complex Ions

Formation of Complex Ions

A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...

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

Correction for Fogal et al., "Mitochondrial p32 Protein Is a Critical Regulator of Tumor Metabolism via Maintenance of Oxidative Phosphorylation".

Molecular and cellular biology·2017

Same author

High throughput gene complementation screening permits identification of a mammalian mitochondrial protein synthesis (ρ(-)) mutant.

Biochimica et biophysica acta·2016

Same author

Mitochondrial disease associated with complex I (NADH-CoQ oxidoreductase) deficiency.

Journal of inherited metabolic disease·2014

Same author

Mitochondrial dysfunction impairs tumor suppressor p53 expression/function.

The Journal of biological chemistry·2011

Same author

Mitochondrial p32 protein is a critical regulator of tumor metabolism via maintenance of oxidative phosphorylation.

Molecular and cellular biology·2010

Same author

Suppression of tumor growth in vivo by the mitocan alpha-tocopheryl succinate requires respiratory complex II.

Clinical cancer research : an official journal of the American Association for Cancer Research·2009

Search research articles

Related Experiment Video

Updated: Jun 9, 2026

Use of Primary Cultured Hippocampal Neurons to Study the Assembly of Axon Initial Segments

Use of Primary Cultured Hippocampal Neurons to Study the Assembly of Axon Initial Segments

Published on: February 12, 2021

Assembling complex I with ACAD9.

Immo E Scheffler¹

¹University of California, San Diego, La Jolla, 92093-0322, USA. ischeffler@ucsd.edu

Cell Metabolism

|September 7, 2010

Summary

This summary is machine-generated.

Acyl-Co dehydrogenase 9 (ACAD9) is essential for mitochondrial complex I assembly, not just fatty acid oxidation. Mutations in ACAD9 cause complex I deficiency in some mitochondrial disease patients.

More Related Videos

The MultiBac Protein Complex Production Platform at the EMBL

The MultiBac Protein Complex Production Platform at the EMBL

Published on: July 11, 2013

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

Related Experiment Videos

Last Updated: Jun 9, 2026

Use of Primary Cultured Hippocampal Neurons to Study the Assembly of Axon Initial Segments

Use of Primary Cultured Hippocampal Neurons to Study the Assembly of Axon Initial Segments

Published on: February 12, 2021

The MultiBac Protein Complex Production Platform at the EMBL

The MultiBac Protein Complex Production Platform at the EMBL

Published on: July 11, 2013

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

Area of Science:

Biochemistry
Molecular Biology
Genetics

Background:

Acyl-Co dehydrogenase 9 (ACAD9) was traditionally associated with fatty acid oxidation.
Mitochondrial diseases are often linked to defects in the electron transport chain.

Discussion:

Nouws et al. (2010) identified a critical, previously unrecognized function of ACAD9 in the assembly of mitochondrial respiratory chain complex I.
This finding redefines the known biological roles of ACAD9.

Key Insights:

ACAD9 is indispensable for the proper formation of mitochondrial complex I.
Specific mutations in the ACAD9 gene lead to isolated complex I deficiency.
This implicates ACAD9 as a key player in the pathogenesis of certain mitochondrial disorders.

Outlook:

Further research into ACAD9's role could reveal new therapeutic targets for mitochondrial diseases.
Understanding ACAD9 function may aid in diagnosing patients with unexplained complex I deficiencies.