| Literature DB >> 11557047 |
C M Hilkens1, H Is'harc, B F Lillemeier, B Strobl, P A Bates, I Behrmann, I M Kerr.
Abstract
The terminal portion of the Janus kinases (Jaks) contains a divergent FERM (Four-point-one, Ezrin, Radixin, Moesin) homology domain comprising 19 conserved hydrophobic regions. To determine the role of this domain in governing recruitment of Jak1, but not Jak3, to the gp130 subunit of the interleukin-6 family of cytokine receptors, the interaction of three Jak1/Jak3 chimeras with gp130 was investigated. Chimeras 1, 2 and 3 (Jak1 FERM regions 1-19, 1-18 and 1-8/Jak3, respectively) were all enzymically active. Chimeras 1 and 2 interacted with the cytoplasmic domain of gp130, although less efficiently than Jak1. Only chimera 2, however, restored gp130 signalling in Jak1-negative cells. The data are consistent with recruitment of Jak1 to gp130 through the Jak1 FERM domain, but also emphasise the likely requirement for precise Jak/receptor orientation to sustain function.Entities:
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Year: 2001 PMID： 11557047 DOI： 10.1016/s0014-5793(01)02783-1
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124