Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2001 Nov;8(5):959-69.
doi: 10.1016/s1097-2765(01)00398-7.

Unexpected effects of FERM domain mutations on catalytic activity of Jak3: structural implication for Janus kinases

Y J Zhou  1 , M Chen, N A Cusack, L H Kimmel, K S Magnuson, J G Boyd, W Lin, J L Roberts, A Lengi, R H Buckley, R L Geahlen, F Candotti, M Gadina, P S Changelian, J J O'Shea
Affiliations
Free article

Unexpected effects of FERM domain mutations on catalytic activity of Jak3: structural implication for Janus kinases

Y J Zhou et al. Mol Cell. 2001 Nov.
Free article

Abstract

Janus kinases comprise carboxyterminal kinase, pseudokinase, SH2-like, and N-terminal FERM domains. We identified three patient-derived mutations in the FERM domain of Jak3 and investigated the functional consequences of these mutations. These mutations inhibited receptor binding and also abrogated kinase activity, suggesting interactions between the FERM and kinase domains. In fact, the domains were found to physically associate, and coexpression of the FERM domain enhanced activity of the isolated kinase domain. Conversely, staurosporine, which alters kinase domain structure, disrupted receptor binding, even though the catalytic activity of Jak3 is dispensable for receptor binding. Thus, the Jak FERM domain appears to have two critical functions: receptor interaction and maintenance of kinase integrity.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

MeSH terms

LinkOut - more resources