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Lactacystin-induced apoptosis of cultured mouse cortical neurons is associated with accumulation of PTEN in the detergent-resistant membrane fraction

journal contribution
posted on 2023-05-17, 01:42 authored by Cheung, NS, Choy, MS, Halliwell, B, Teo, TS, Bay, BH, Lee, AY, Qi, RZ, Koh, VH, Whiteman, M, Koay, ES, Chiu, LL, Zhu, HJ, Wong, KP, Beart, PM, Cheng, HC
The tumor suppressor function of PTEN is attributed to its phospholipid phosphatase activity that dephosphorylates the plasma membrane phosphatidylinositol-(3,4,5)-triphosphate [PtdIns(3,4,5)P3]. Implicit in this notion is that PTEN needs to be targeted to the plasma membrane to dephosphorylate PtdIns(3,4,5)P3. However, the recruitment of PTEN to the plasma membrane is not fully understood. Here, we demonstrate PTEN accumulation in the detergent-insoluble fraction of neuronal cells in response to treatment by the proteasome inhibitor lactacystin. First, lactacystin induces apoptosis and the activation of caspase-3 in cultured cortical neurons. Second, PTEN undergoes proteolysis to form a truncated 50-kDa form that lacks parts of its C-terminal tail. Third, the truncated PTEN is stably associated with the detergent-insoluble fraction in which the plasma membrane marker protein flotillin-1 resides. Taken together, our results suggest that truncation and accumulation of PTEN to the detergent-insoluble membrane fraction are two events associated with the apoptotic signals of the proteasome inhibitor in cortical neurons.

History

Publication title

Cellular and Molecular Life Sciences

Volume

61

Issue

15

Pagination

1926-1934

ISSN

1420-682X

Department/School

Menzies Institute for Medical Research

Publisher

Birkhauser Verlag Ag

Place of publication

Viadukstrasse 40-44, Po Box 133, Basel, Switzerland, Ch-4010

Repository Status

  • Restricted

Socio-economic Objectives

Clinical health not elsewhere classified

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