background:
Presenilins associated rhombiod-like protein (PARL) is a mitochondrial intramembrane-cleaving protease belonging to the S54 family of proteins. PARL is involved in intramembrane regulated proteolysis as its catalytic activity involves the cleaving of signaling proteins at intracellular membranes to release active fragments in signal transduction cascades. Using a triad of histidine, serine and asparagine, PARL cleaves type-1 transmembrane domains. PARL is a multi-pass membrane protein localizing to the inner and outer mitochondrial membranes, but it can also be detected in the nucleus following proteolytical processing of P-β. PARL co-localizes with the presenilins PSEN1 and PSEN2, the familial Alzheimer disease products.
Function:
Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptoptic signals (By similarity). Promotes changes in mitochondria morphology regulated by phosphorylation of P-beta domain.
Subcellular Location:
Mitochondrion inner membrane and Nucleus. Translocated into the nucleus by an unknown mechanism.
Post-translational modifications:
P-beta is proteolytically processed (beta-cleavage) in a PARL-dependent manner. The cleavage is inhibited when residues Ser-65, Thr-69 and Ser-70 are all phosphorylated.
Similarity:
Belongs to the peptidase S54 family.
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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