USP15

A gene on chromosome 12q14 that encodes an enzyme which deubiquitinates Lys-48-linked polyubiquitinated proteins, targeting them against proteasomal degradation. USP15 protects APC and HPV type-16 protein E6 against degradation via the ubiquitin proteasome pathway. It is expressed in skeletal muscle, kidneys, heart, placenta, liver, thymus, lungs and ovaries.

References in periodicals archive ?

USP15, which is highly similar with USP4 [69], also is involved in Wnt signaling and bone formation [91].

USP15, which regulates osteoblast function and bone formation, is connected to osteoclast function too [76].

To date, several DUBs are found to regulate osteoblast function (USP4, USP7, USP9x, USP15, UCH-l3, and MYSM1) and osteoclast function (CYLD, USP15, USP18, A20, and POH1) (Table 2).

Gonzalez-Junca et al., "USP15 stabilizes TGF-[beta] receptor I and promotes oncogenesis through the activation of TGF-[beta] signaling in glioblastoma," Nature Medicine, vol.

Dingwell et al., "USP15 targets ALK3/BMPR1A for deubiquitylation to enhance bone morphogenetic protein signalling," Open Biology, vol.

Deubiquitinating Enzymes and Bone Remodeling

dUb Target Ubiquitin-mediated Biological molecules modifications function A20 RIP1, RIP2, TRAF2, K63 Signaling TRAF6, MALT1, NEMO termination CYLD MyD88, TRAF2, K63 Signaling TRAF6, TRAF7, termination RIP1, NEMO USP2[alpha] TRAF6 K63 Signaling termination USP4 TRAF2, TRAF6, TAK1 K63 Signaling termination USP7 TRAF6, NEMO K63 Signaling termination USP10 TRAF6, NEMO K63/M1 Signaling termination USP11 IxBa K48 Proteolytic degradation USP15 IxBa K48 Proteolytic degradation USP18 TAK1, NEMO K63 Signaling termination USP21 RIP1 K63 Signaling termination USP25 TRAF2, TRAF3, K63/K48 Signaling TRAF5, TRAF6 termination/ proteolytic degradation Table 4: TLR expression profile.

Interplay between Inflammation and Sternness in Cancer Cells: The Role of Toll-Like Receptor Signaling

Joan Seoane , Director of Translational Research at the Vall d'Hebron Institute of Oncology (VHIO) and ICREA Research Professor identified USP15 as a critical protein in cancer which, thanks to its molecular characteristics, shows enormous therapeutic promise.

USP15 promotes tumor progression by activating the TGFa pathway.

Seoane's team has unmasked the USP15 enzyme as activator of the TGFa chain reaction.

USP15 acts by controlling and correcting the TGFa activity in the same way that a thermostat regulates temperature.