maintenance of protein location in cell
Definition
Target type: biologicalprocess
Any process in which a protein is maintained in a specific location within, or in the membrane of, a cell, and is prevented from moving elsewhere. [GOC:isa_complete, GOC:mah]
The maintenance of protein location in a cell, also known as protein localization or protein trafficking, is a complex and essential biological process that ensures proteins are delivered to their correct destinations within the cell. This process is crucial for the proper functioning of cellular pathways, signaling networks, and overall cellular organization. Here's a breakdown of the key steps involved:
1. **Protein Synthesis and Folding:** Protein synthesis begins in the cytoplasm, specifically on ribosomes. As the protein is being synthesized, it starts to fold into its three-dimensional structure, which is critical for its function and localization.
2. **Signal Sequences and Sorting:** Proteins destined for specific cellular compartments often contain signal sequences, short stretches of amino acids that act as "zip codes" directing them to their target destinations. These signals can be located at the N-terminus (beginning), C-terminus (end), or within the protein sequence.
3. **Protein Translocation:** The process of moving proteins across membranes is known as translocation. This can occur through:
- **Translocation across the Endoplasmic Reticulum (ER) Membrane:** Proteins destined for the ER, Golgi apparatus, lysosomes, or secretion are often translocated into the ER lumen during synthesis. This process involves a protein translocator complex embedded in the ER membrane.
- **Translocation into Mitochondria:** Proteins targeted to mitochondria have specific signal sequences recognized by import receptors on the outer mitochondrial membrane. They are then translocated through the mitochondrial translocases (TOM and TIM complexes).
- **Translocation into the Nucleus:** Nuclear localization signals (NLSs) guide proteins to the nucleus. These signals interact with import receptors on the nuclear pore complex, allowing the proteins to enter the nucleus.
4. **Sorting in the Golgi Apparatus:** The Golgi apparatus acts as a central sorting station for proteins. After passing through the ER, proteins move through the Golgi compartments, where they may undergo further modifications, such as glycosylation, phosphorylation, or proteolytic processing. These modifications can help in protein sorting and localization.
5. **Vesicular Transport:** Many proteins are packaged into small membrane-bound vesicles that bud off from the Golgi or other organelles. These vesicles carry their cargo to specific destinations within the cell. Vesicle trafficking relies on a complex network of proteins, including Rab GTPases, SNAREs, and motor proteins, that ensure accurate and efficient delivery.
6. **Targeting and Anchoring:** Once a protein reaches its final destination, it must be anchored or retained in that compartment. This can involve interactions with other proteins, lipids, or specific cellular structures. For example, membrane-bound proteins can be tethered to the membrane by transmembrane domains or lipid modifications.
7. **Protein Degradation:** Proteins that are misfolded or no longer needed are targeted for degradation by proteasomes or lysosomes. This process helps to maintain cellular homeostasis and prevent the accumulation of potentially harmful proteins.
The maintenance of protein location is a dynamic and tightly regulated process that relies on a complex interplay of protein synthesis, folding, translocation, sorting, vesicle trafficking, and targeted anchoring. Dysregulation of this process can lead to various cellular malfunctions and diseases.'
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Proteins (1)
Protein | Definition | Taxonomy |
---|---|---|
T-cell surface glycoprotein CD4 | A CD4 molecule that is encoded in the genome of human. [PRO:DNx, UniProtKB:P01730] | Homo sapiens (human) |
Compounds (1)
Compound | Definition | Classes | Roles |
---|---|---|---|
complestatin | chloropeptin II : A heterodetic cyclic peptide consisting of N-acylated trytophan, 3,5-dichloro-4-hydroxyphenylglycine, 4-hydroxyphenylglycine, 3,5-dichloro-4-hydroxyphenylglycyl, tyrosine and 4-hydroxyphenylglycine residues joined in sequence and in which the side-chain of the central 4-hydroxyphenylglycine residue is attached to the side-chain of the tryptophan via a C3-C6 bond and to the side-chain of the tyrosine via an ether bond from C5. It is isolated from the culture broth of Streptomyces and has anti-HIV-1 activity. complestatin: compound extracted from Streptomyces lavendulae mycelia; on acid hydrolysis yields D-4-hydroxyphenylglycine & D-3,5-dichloro-4-hydroxyphenylglycine & acidic chromophore; inhibits gp120-CD4 binding isocomplestatin : A heterodetic cyclic peptide which is a atropisomer of complestatin. It is isolated from the culture broth of Streptomyces and has anti-HIV-1 activity. | cyclic ether; heterodetic cyclic peptide; indoles; organic heterobicyclic compound; organochlorine compound; peptide antibiotic; polyphenol | anti-HIV-1 agent; antimicrobial agent; HIV-1 integrase inhibitor; metabolite |