Target type: biologicalprocess
The process in which a SUMO protein (small ubiquitin-related modifier) is cleaved from its target protein. [GOC:jl, PMID:11265250]
Protein desumoylation is a crucial biological process that involves the removal of SUMO (Small Ubiquitin-like Modifier) proteins from target proteins. SUMOylation, the attachment of SUMO proteins, is a reversible post-translational modification that plays a vital role in regulating various cellular processes, including protein stability, localization, and interactions. Desumoylation is mediated by a family of enzymes called SUMO proteases or SENPs (Sentrin/SUMO-specific proteases). These enzymes recognize and cleave the isopeptide bond between the SUMO protein and its target, releasing the SUMO moiety and restoring the target protein to its unmodified state. The process begins with the recognition of the SUMO-conjugated target protein by the SENP. The enzyme then utilizes its catalytic cysteine residue to attack the isopeptide bond between SUMO and the target protein, leading to the formation of a thioester intermediate. Subsequently, a water molecule attacks the thioester bond, releasing the SUMO protein and regenerating the active SENP enzyme. Desumoylation plays critical roles in various biological processes, including: * **Transcriptional regulation:** Desumoylation of transcription factors can modulate their activity, influencing gene expression. * **DNA repair:** Desumoylation is essential for efficient DNA damage repair mechanisms. * **Apoptosis:** Desumoylation can regulate the apoptotic pathway, contributing to cell death. * **Signaling pathways:** Desumoylation can modulate the activity of signaling proteins, impacting cellular responses. * **Protein stability:** Desumoylation can influence protein stability, promoting either degradation or protection from degradation. Dysregulation of desumoylation has been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. In summary, desumoylation is a critical cellular process that dynamically regulates the activity and fate of target proteins. It involves the precise action of SUMO proteases, SENPs, which catalyze the removal of SUMO proteins from their targets, ultimately impacting a wide range of cellular functions and contributing to overall cellular homeostasis.'
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Protein | Definition | Taxonomy |
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Sentrin-specific protease 1 | A sentrin-specific protease 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9P0U3] | Homo sapiens (human) |
Sentrin-specific protease 2 | A sentrin-specific protease 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9HC62] | Homo sapiens (human) |
Sentrin-specific protease 6 | A sentrin-specific protease 6 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9GZR1] | Homo sapiens (human) |
Histidine triad nucleotide-binding protein 1 | An adenosine 5-monophosphoramidase HINT1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P49773] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
streptonigrin | pyridines; quinolone | antimicrobial agent; antineoplastic agent | |
ursolic acid | hydroxy monocarboxylic acid; pentacyclic triterpenoid | geroprotector; plant metabolite | |
Tormentic acid | tormentic acid: aglycone of Rosamultin | triterpenoid | metabolite |
atromentin | atromentin : A member of the class of dihydroxy-1,4-benzoquinones that is 2,5-dihydroxycyclohexa-2,5-diene-1,4-dione which is substituted by a 4-hydroxyphenyl group at positions 3 and 6. It is a mushroom pigment isolated from several fungi species and acts as a smooth muscle stimulant, and exhibits anticoagulant, antibacterial and antineoplastic properties. atromentin: an enoyl-ACP reductase (FabK) inhibitor; isolated from Streptococcus pneumoniae; structure in first source | dihydroxy-1,4-benzoquinones; polyphenol | antibacterial agent; anticoagulant; antineoplastic agent; apoptosis inducer; biological pigment; EC 1.3.1.9 [enoyl-[acyl-carrier-protein] reductase (NADH)] inhibitor; fungal metabolite |
scoparianoside b | scoparianoside B: isolated from the fruit of Japanese Kochia scoparia; structure given in first source | triterpenoid saponin | |
pomolic acid | pomolic acid: from Rosa woodsii & Hyptis capitata; structure in first source | triterpenoid | metabolite |
vialinin a | vialinin A: free radical scavenger from an edible mushroom in China; structure in first source | ||
gn6958 | GN6958: inhibits SUMO-sentrin specific protease 1 (SENP1); structure in first source | ||
guanosine monophosphate | guanosine 5'-monophosphate : A purine ribonucleoside 5'-monophosphate having guanine as the nucleobase. Guanosine Monophosphate: A guanine nucleotide containing one phosphate group esterified to the sugar moiety and found widely in nature. | guanosine 5'-phosphate; purine ribonucleoside 5'-monophosphate | biomarker; Escherichia coli metabolite; metabolite; mouse metabolite |