Importin Beta Plays an Essential Role in the Regulation of the LysRS-Ap4A Pathway in Immunologically Activated Mast Cells | Zendy

Irit Carmi-Levy | Zendy; Alex Motzik | Zendy; Yifat OfirBirin | Zendy; Zohar Yagil | Zendy; Christopher Maolin Yang | Zendy; D.M. Kemeny | Zendy; Jung Min Han | Zendy; SungHoon Kim | Zendy; Gillian Kay | Zendy; Hovav Nechushtan | Zendy; Ryo Suzuki | Zendy; Juan Rivera | Zendy; Ehud Razin | Zendy

Open Access

Importin Beta Plays an Essential Role in the Regulation of the LysRS-Ap₄A Pathway in Immunologically Activated Mast Cells

Author(s) -

Irit Carmi-Levy,

Alex Motzik,

Yifat OfirBirin,

Zohar Yagil,

Christopher Maolin Yang,

D.M. Kemeny,

Jung Min Han,

SungHoon Kim,

Gillian Kay,

Hovav Nechushtan,

Ryo Suzuki,

Juan Rivera,

Ehud Razin

Publication year - 2011

Publication title -

molecular and cellular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.14

H-Index - 327

eISSN - 1067-8824

pISSN - 0270-7306

DOI - 10.1128/mcb.01159-10

Subject(s) - biology , microphthalmia associated transcription factor , hydrolase , transcription factor , microbiology and biotechnology , gene silencing , enzyme , biochemistry , gene

We recently reported that diadenosine tetraphosphate hydrolase (Ap4 A hydrolase) plays a critical role in gene expression via regulation of intracellular Ap4 A levels. This enzyme serves as a component of our newly described lysyl tRNA synthetase (LysRS)-Ap4 A biochemical pathway that is triggered upon immunological challenge. Here we explored the mechanism of this enzyme's translocation into the nucleus and found its immunologically dependent association with importin beta. Silencing of importin beta prevented Ap4 A hydrolase nuclear translocation and affected the local concentration of Ap4 A, which led to an increase in microphthalmia transcription factor (MITF) transcriptional activity. Furthermore, immunological activation of mast cells resulted in dephosphorylation of Ap4 A hydrolase, which changed the hydrolytic activity of the enzyme.

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