Anti-ZMPSTE24 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

ZMPSTE24 also known as FACE1 or STE24 is a zinc metalloprotease enzyme involved in the post-translational modification of prelamin A to mature lamin A. This enzyme specifically cleaves the C-terminal tail of prelamin A a critical step required for proper nuclear envelope structure and function. ZMPSTE24 has a molecular mass of approximately 54 kDa and is expressed in several tissues including skeletal muscle heart and skin. Its activity primarily takes place in the endoplasmic reticulum membrane where it executes its proteolytic functions.

Biological function summary

The alteration of prelamin A to lamin A by ZMPSTE24 is necessary for maintaining nuclear shape and stability. Lamin A is a major component of the nuclear lamina providing structural support to the nuclear envelope. ZMPSTE24 is part of a proteolytic complex that ensures the proper maturation of lamin A which plays a significant role in DNA replication and cellular division. Deficiency in ZMPSTE24 activity can lead to the accumulation of farnesylated prelamin A disrupting nuclear architecture and cellular processes.

Pathways

The function of ZMPSTE24 integrates into the broader context of the lamin A maturation pathway significant for nuclear integrity. It collaborates with other enzymes like farnesyltransferase and icmt during the maturation process of prelamin A to lamin A. ZMPSTE24 also interacts with the protein lamin B which is an associate in the nuclear lamina. This cooperation within the pathway ensures the functional execution of nuclear mechanical properties and DNA repair processes.

Associated diseases and disorders

The abnormal function or mutation of ZMPSTE24 connects direly with disorders such as restrictive dermopathy and Hutchinson-Gilford progeria syndrome (HGPS). In HGPS defective ZMPSTE24 fails to process prelamin A leading to the build-up of a toxic version of prelamin A termed progerin. This accumulation contributes to premature aging phenotypes. The disorder correlates with mutations in LMNA a gene encoding lamins A and C highlighting the tandem dependency between ZMPSTE24 and lamin A in maintaining nuclear structure and overall cellular health.