Page last updated: 2024-10-24

protein K6-linked deubiquitination

Definition

Target type: biologicalprocess

A protein deubiquitination process in which a K6-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 6 of the ubiquitin monomers, is removed from a protein. [GOC:sp]

K6-linked deubiquitination is a specialized form of ubiquitin chain processing that involves the removal of K6-linked polyubiquitin chains from target proteins. Ubiquitination is a crucial cellular process that regulates a vast array of cellular functions, including protein degradation, signal transduction, and DNA repair. Ubiquitin chains can be assembled with various linkage types, and K6-linked ubiquitination represents a distinct chain type with unique functional consequences.

The process of K6-linked deubiquitination is catalyzed by specific deubiquitinases (DUBs), which are enzymes that cleave ubiquitin chains from target proteins. DUBs possess specific substrate recognition domains that enable them to distinguish between different ubiquitin chain types, ensuring that K6-linked deubiquitination occurs selectively.

K6-linked deubiquitination plays a critical role in various cellular pathways. For instance, it is involved in regulating the stability and activity of specific proteins, controlling DNA repair processes, and influencing immune responses. The precise function of K6-linked deubiquitination often depends on the context and the specific proteins involved.

K6-linked deubiquitination is tightly regulated, ensuring its proper function. Cellular signaling pathways, including phosphorylation cascades, can influence the activity of K6-specific DUBs. Additionally, the expression levels of DUBs and their substrates are often regulated to fine-tune the process of K6-linked deubiquitination.

Dysregulation of K6-linked deubiquitination can contribute to various disease states. For instance, aberrant K6-linked deubiquitination has been implicated in cancer development and progression, as well as neurodegenerative disorders.

In summary, K6-linked deubiquitination is a specialized and highly regulated cellular process that involves the removal of K6-linked ubiquitin chains from target proteins. This process plays a crucial role in diverse cellular pathways, influencing protein stability, signal transduction, DNA repair, and immune responses. Dysregulation of K6-linked deubiquitination can contribute to various disease states, highlighting its significance in maintaining cellular homeostasis.'
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Proteins (1)

ProteinDefinitionTaxonomy
Ubiquitin carboxyl-terminal hydrolase 13A ubiquitin carboxyl-terminal hydrolase 13 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q92995]Homo sapiens (human)

Compounds (1)

CompoundDefinitionClassesRoles
spautin-1