Journal
JOURNAL OF CELL SCIENCE
Volume 118, Issue 15, Pages 3431-3443Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.02472
Keywords
dynein light chain; rp3; SATB 1; nuclear matrix; Bcl2
Categories
Funding
- NEI NIH HHS [EY11307, R01 EY011307] Funding Source: Medline
Ask authors/readers for more resources
Cytoplasmic dynein is a motor protein complex involved in microtubule-based cargo movement. Previous biochemical evidence suggests that dynein light chain subunits also exist outside the dynein complex. Here we show that the dynein light chain rp3 is present in both the cytoplasm and the nucleus. Nuclear rp3 binds to and assembles with the transcription factor SATB1 at nuclear matrix-associated structures. Dynein intermediate chain was also detected in the nucleus, but it was dispensable for the rp3-SATBl interaction. SATB1 facilitates the nuclear localization of rp3, whereas rp3 and dynein motor activity are not essential for nuclear accumulation of SATB1. The nuclear rp3-SATBl protein complex is assembled with a DNA element of the matrix attachment region of the Bcl2 gene. Finally, rp3 is involved in SATB1-mediated gene repression of Bcl2. Our data provide evidence that dynein subunit rp3 has functions independent of the dynein motor.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available