Journal
CANCER RESEARCH
Volume 67, Issue 21, Pages 10207-10213Publisher
AMER ASSOC CANCER RESEARCH
DOI: 10.1158/0008-5472.CAN-07-2574
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Funding
- NCI NIH HHS [CA099147, CA099187] Funding Source: Medline
- NIEHS NIH HHS [ES014399, ES013340, ES012063] Funding Source: Medline
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dWe have previously identified murine lung adenoma susceptibility I (Las1) as the pulmonary adenoma susceptibility 1 candidate gene. Last has two natural alleles, Las1-A/J and Las1-B6. Las1 encodes an 85-kDa protein with uncharacterized biological function. In the present study, we report that Last is an unstable protein and the rapid destruction of Last depends on the ubiquitin-proteasome pathway. Last is a new microtubule-binding protein and Last associated with tubulin is not ubiquitinated. We further show that Las1-A/J is a more stable protein than Las1-B6. Last is expressed in the G(2) phase of the cell cycle and that ubiquitin-proteasome-mediated Las1 destruction occurs in mitosis. Overexpression of Las1-A/J inhibits normal E10 cell proliferation and induces a defective cytokinesis. The differential degradation of Las1-A/J and LasB6 has important implications for its intracellular function and may eventually explain Las1-A/J in lung tumorigenesis.
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