Journal article

ATM Substrate Chk2-interacting Zn2 Finger (ASCIZ) Is a Bi-functional Transcriptional Activator and Feedback Sensor in the Regulation of Dynein Light Chain (DYNLL1) Expression

Sabine Jurado, Lindus A Conlan, Emma K Baker, Jane-Lee Ng, Nora Tenis, Nicolas C Hoch, Kimberly Gleeson, Monique Smeets, David Izon, Joerg Heierhorst

JOURNAL OF BIOLOGICAL CHEMISTRY | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2012

Abstract

The highly conserved DYNLL1 (LC8) protein was originally discovered as a light chain of the dynein motor complex, but is increasingly emerging as a sequence-specific regulator of protein dimerization with hundreds of targets and wide-ranging cellular functions. Despite its important roles, DYNLL1's own regulation remains poorly understood. Here we identify ASCIZ (ATMIN/ZNF822), an essential Zn(2+) finger protein with dual roles in the DNA base damage response and as a developmental transcription factor, as a conserved regulator of Dynll1 gene expression. DYNLL1 levels are reduced by ∼10-fold in the absence of ASCIZ in human, mouse and chicken cells. ASCIZ binds directly to the Dynll1 promote..

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Grants

Funding Acknowledgements

This work was supported by grants and a Senior Research Fellowship from the National Health and Medical Research Council (NHMRC) of Australia (to J. H.), a PhD scholarship from the Cooperative Research Centre Cancer Therapeutics (to S. J.), and in part by the Victorian Government's Operational Infrastructure Support Program.