Ubiquitin specific peptidase 17-like family member 22 (USP17L22)

Ubiquitin specific peptidase 17-like family member 22 (USP17L22) is a putative cysteine protease belonging to the deubiquitinating enzyme (DUB) family known as ubiquitin-specific proteases (USPs). DUBs hydrolyze ubiquitin from substrate proteins, thereby regulating protein degradation, cellular localization, and activity. USP17L22, like other members of the USP17 subfamily, is thought to regulate cellular processes such as cell cycle progression, migration, and cytoskeletal dynamics by deubiquitinating key regulatory proteins including CDC25A, SETD8, and small GTPases involved in cell motility[2][4]. Although USP17 paralogs—including USP17—are described as therapeutic targets in cancer and inflammation, direct data for USP17L22 itself is insufficient or lacking. The molecular and functional properties of USP17L22 are assumed to be similar to other USP17 family members, but it is not an established or commonly studied target.

Other names

Ubiquitin carboxyl-terminal hydrolase 17-like protein 22USP17L22

None documented for USP17L22. Potential mechanisms for therapeutic targeting (based on USP17 family): Inhibition of deubiquitinating activity to block cell proliferation or migration; Interference with GTPase membrane localization or Ras signaling.