karyopherin

(redirected from Karyopherins)

karyopherin

(kar-ē-of'ĕr-in),
A type of soluble protein active in the complexes of nuclear pores.
[karyo- + G. pherō, to carry, + -in]
References in periodicals archive ?
(2017) Karyopherins regulate nuclear pore complex barrier and transport function.
(20, 21) Several groups independently and almost simultaneously identified these two types of NTRs, and named the molecules importin [alpha] or karyopherin [alpha] for PTAC58 and importin [beta] or karyopherin [beta] for PTAC97.
Importin [alpha], also known as karyopherin [alpha] (KPNA), was first identified as an adaptor protein linking cNLS-containing proteins with importin [beta], also called karyopherin [beta] (KPNB).
(2017) Karyopherin Alpha Proteins Regulate Oligodendrocyte Differentiation.
(2016) Karyopherin alpha 1 regulates satellite cell proliferation and survival by modulating nuclear Import.
(2004) The bipartite nuclear localization sequence of Rpn2 is required for nuclear import of proteasomal base complexes via karyopherin [alpha][beta] and proteasome functions.
However, molecules larger than 50 kDa require machinery whereby mobile targeting receptors called karyopherins recognize and bind to receptor-mediated intracellular signals through specific signal sequences that are present on substrate proteins.
Karyopherins recognize various cargo molecules and bind to them by interacting with NLS or NES present on cargo molecules.
It binds to importin [alpha]3 and importin [alpha]6 and is actively transported into the nucleus with the help of these karyopherins [44].
Since NF-[kappa]B and AP-1 activity can also be inhibited by GR, it is likely that GR has a higher affinity for the karyopherins than the inflammatory transcription factors and/or activated GR induces the production of endogenous inhibitors of importins involved in the translocation of inflammatory transcription factors.
However, additional knowledge regarding the precise control over the recruitment and activation of a few key karyopherins could be beneficial in the development of better therapeutic approaches.
Cleavage stage porcine embryos may have differing developmental requirements for karyopherins alpha2 and alpha3.