alexa Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene, interacts with tuberin and appears to be localized to cytoplasmic vesicles.
Molecular Biology

Molecular Biology

Journal of Cytology & Histology

Author(s): Plank TL, Yeung RS, Henske EP

Abstract Share this page

Abstract Tuberous sclerosis is an inherited syndrome associated with mutations in two tumor suppressor genes: TSC1 and TSC2. Tuberin, the product of TSC2, appears to be localized to the Golgi apparatus and may have a function in vesicular transport. The function of hamartin, the product of TSC1, is not known. In this report, we demonstrate an interaction between hamartin and tuberin, which is detectable at endogenous protein levels. Hamartin is present in a cell line derived from the Eker rat that lacks functional tuberin, indicating that the stability of hamartin is not dependent on its interaction with tuberin. Hamartin is localized to the membrane/particulate (P100) fraction of cultured cells. The P100 localization is unchanged in the Eker cells. Finally, we show that at endogenous expression levels, hamartin has a punctate pattern of immunofluorescence in the cytoplasm. Taken together, the presence of hamartin in the membrane/particulate fraction and its pattern of cytoplasmic staining suggest that it is localized to cytoplasmic vesicles. If altered vesicular trafficking leads to tumorigenesis in tuberous sclerosis, TSC1 and TSC2 may have a novel mechanism of tumor suppression.
This article was published in Cancer Res and referenced in Journal of Cytology & Histology

Relevant Expert PPTs

Relevant Speaker PPTs

Peer Reviewed Journals
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version