protein modification by small protein removal
Definition
Target type: biologicalprocess
A protein modification process in which one or more covalently attached groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are removed from a target protein. [GOC:mah]
Protein modification by small protein removal is a crucial biological process that involves the precise removal of small protein segments, often peptides or amino acid residues, from a larger protein. This process can dramatically alter the protein's structure, function, and interactions. Here's a detailed breakdown of the biological mechanisms involved:
1. **Target Recognition:** The first step is the recognition of the specific target protein by dedicated enzymes or protein complexes. These enzymes often have highly specific binding sites that recognize unique sequences or structural features within the target protein.
2. **Cleavage and Removal:** Once bound, the enzyme performs a precise cleavage event, removing the designated small protein segment from the target protein. This cleavage can be mediated by different enzymatic mechanisms, such as proteases, peptidases, or deubiquitinases, depending on the specific type of modification.
3. **Post-Cleavage Events:** The removal of the small protein segment can trigger a cascade of events that influence the target protein's fate. Some common consequences include:
a. **Altered Structure and Conformation:** Removal of specific amino acids can significantly alter the protein's three-dimensional shape, impacting its activity and interactions with other molecules.
b. **Functional Activation or Deactivation:** The small protein segment may be an inhibitor or activator of the target protein. Its removal can switch the protein's activity on or off.
c. **Signal Transduction:** The removed segment can act as a signaling molecule itself, triggering downstream cellular processes.
d. **Protein Stability and Degradation:** The removal event can affect the target protein's stability, leading to its degradation through cellular pathways.
4. **Regulation and Control:** Protein modification by small protein removal is tightly regulated by various factors, including cellular conditions, signaling pathways, and environmental cues. This regulation ensures that the process occurs at the right time and place, contributing to cellular homeostasis.
5. **Examples and Importance:** This process plays critical roles in many cellular functions, including:
a. **Signal Transduction:** Removal of small proteins can activate or deactivate signaling cascades, regulating cell growth, differentiation, and response to stress.
b. **Immune Response:** Proteolytic processing of immune proteins, such as cytokines and chemokines, fine-tunes immune responses.
c. **Development and Differentiation:** The controlled removal of small proteins influences the development and differentiation of cells and tissues.
d. **Cellular Regulation:** This process plays a critical role in controlling protein activity, stability, and localization within cells.
Protein modification by small protein removal is a highly dynamic and intricate process with profound implications for cellular function and regulation. Understanding this mechanism is essential for elucidating the complexity of cellular life and for developing strategies for therapeutic intervention in disease states.'
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Proteins (1)
Protein | Definition | Taxonomy |
---|---|---|
Sentrin-specific protease 6 | A sentrin-specific protease 6 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9GZR1] | Homo sapiens (human) |
Compounds (1)
Compound | Definition | Classes | Roles |
---|---|---|---|
streptonigrin | pyridines; quinolone | antimicrobial agent; antineoplastic agent |