Function
Speckle-type POZ (pox virus and zinc finger) protein (SPOP) is an adaptor of the cullin-3-based ubiquitin ligase responsible for the degradation of oncoproteins which are overexpressed in many tumor cells[1]. SPOP forms nuclear foci after DNA damage at DNA double-strand break sites. SPOP interacts with bromodomain proteins via their MATH (Meprin And TRAP Homology) domain and regulate them.
Disease
SPOP mutations contribute to prostate cancer development by altering the steady-state levels of key components in the androgen-signaling pathway [2].
Structural highlights
The 3D structure of SPOP MATH domain complex with bromodomain (BRD3) peptide shows the with the prostate cancer-associated mutations located at SPOP residues forming H-bonds or hydrophobic contacts with BRD3 and the endometrial-associated (uterus-associated) [3].
3D structures of speckle-type POZ protein
Speckle-type POZ protein 3D structures
