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Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

Signal Sequences and Sorting Receptors

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...

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,...

Conserved Binding Sites

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...

Calmodulin-dependent Signaling

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...

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...

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Related Experiment Video

Updated: Dec 31, 2025

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP

Published on: June 15, 2018

COP9 signalosome: Discovery, conservation, activity, and function.

Nanxun Qin^1,2, Dongqing Xu³, Jigang Li⁴

¹State Key Laboratory of Protein and Plant Gene Research, School of Advanced Agricultural Sciences and School of Life Sciences, Peking University, Beijing, 100871, China.

Journal of Integrative Plant Biology

|January 3, 2020

Summary

The COP9 signalosome (CSN) is a key protein complex regulating plant development. This review details its discovery, structure, and vital roles in responding to environmental and hormonal signals.

Keywords:

COP9 signalosome deneddylation photomorphogenesis protein degradation ubiquitin-proteasome pathway

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Area of Science:

Molecular Biology
Plant Science
Developmental Biology

Background:

The COP9 signalosome (CSN) is a conserved protein complex crucial for eukaryotic development.
CSN typically comprises eight subunits in higher eukaryotes and regulates cullin-RING ligase (CRL) activity.
CSN was initially discovered in plants through genetic screens for photomorphogenesis mutants.

Purpose of the Study:

To review the discovery, composition, structure, and function of the CSN complex in plants.
To elucidate CSN's role in regulating plant development.
To summarize CSN's involvement in responses to light, temperature, and phytohormones.

Main Methods:

Literature review and synthesis of existing research on the COP9 signalosome.
Analysis of genetic, molecular, and biochemical studies.
Comparative analysis of CSN across different eukaryotic organisms.

Main Results:

CSN regulates CRL E3 ubiquitin ligase complexes, impacting gene expression, cell proliferation, and cell cycle.
CSN plays critical roles in mediating plant responses to environmental cues like light and temperature.
CSN is essential for integrating internal hormonal signals with developmental pathways.

Conclusions:

The COP9 signalosome is a fundamental regulator of plant growth and development.
Understanding CSN's mechanisms provides insights into plant adaptation and stress responses.
CSN's multifaceted roles highlight its importance in plant biology.