
Alterations in the nucleocytoplasmic transport in apoptosis: Caspases lead the way
Author(s) -
Kopeina Gelina S.,
Prokhorova Evgeniia A.,
Lavrik In.,
Zhivotovsky Boris
Publication year - 2018
Publication title -
cell proliferation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.647
H-Index - 74
eISSN - 1365-2184
pISSN - 0960-7722
DOI - 10.1111/cpr.12467
Subject(s) - caspase , microbiology and biotechnology , apoptosis , proteases , intrinsic apoptosis , programmed cell death , caspase 2 , multicellular organism , cytosol , biology , chemistry , cell , biochemistry , enzyme
Apoptosis is a mode of regulated cell death that is indispensable for the morphogenesis, development and homeostasis of multicellular organisms. Caspases are cysteine‐dependent aspartate‐specific proteases, which function as initiators and executors of apoptosis. Caspases are cytosolic proteins that can cleave substrates located in different intracellular compartments during apoptosis. Many years ago, the involvement of caspases in the regulation of nuclear changes, a hallmark of apoptosis, was documented. Accumulated data suggest that apoptosis‐associated alterations in nucleocytoplasmic transport are also linked to caspase activity. Here, we aim to discuss the current state of knowledge regarding this process. Particular attention will be focused on caspase nuclear entry and their functions in the demolition of the nucleus upon apoptotic stimuli.