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Assessment of Selective mRNA Translation in Mammalian Cells by Polysome Profiling
10:00

Assessment of Selective mRNA Translation in Mammalian Cells by Polysome Profiling

Published on: October 28, 2014

RPL41, a small ribosomal peptide deregulated in tumors, is essential for mitosis and centrosome integrity

Shan Wang1, Jianmin Huang, Jie He

  • 1Department of Pathology, Brigham and Women's Hospital, Harvard Medical School, 75 Francis Street, Boston, MA 02115, USA.

Neoplasia (New York, N.Y.)
|March 18, 2010
PubMed

Insights

Ribosomal large subunit protein 41 (RPL41) acts as a tumor suppressor. Its down-regulation promotes malignant transformation by disrupting microtubule stability, centrosome integrity, and proper cell division.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Oncology

Background:

  • Ribosomal large subunit protein 41 (RPL41) is a small, basic peptide.
  • The function of RPL41 in cellular processes, particularly in cancer, remains largely unexplored.

Purpose of the Study:

  • To investigate the role of RPL41 in cellular transformation and tumor suppression.
  • To elucidate the molecular mechanisms underlying RPL41's function, focusing on its interaction with the cytoskeleton.

Main Methods:

  • Antisense-based screening and small interfering RNA (siRNA) for RPL41 depletion in NIH3T3 cells.
  • Fluorescence in situ hybridization (FISH) and real-time quantitative reverse transcription-polymerase chain reaction (RT-qPCR) to assess RPL41 levels in cell lines and primary tumors.
  • Mass spectrometry and Western blot analysis to identify RPL41 interacting proteins.
  • Functional assays including soft agar colony formation, tumor growth in mice, microtubule depolymerization resistance, cell cycle analysis, and centrosome integrity assessment.

Main Results:

  • RPL41 depletion induced anchorage-independent growth and malignant transformation of NIH3T3 cells, leading to increased tumor growth in mice.
  • RPL41 deletion/down-regulation was frequent in tumor cell lines (59%) and primary breast cancers (75%), suggesting a tumor suppressor role.
  • RPL41 was identified as a microtubule-associated protein, directly binding to polymerized tubulins and stabilizing microtubules.
  • RPL41 depletion caused abnormal mitosis, cytokinesis failure, polynuclear cells, and premature centrosome splitting, indicating disrupted spindle function and centrosome integrity.

Conclusions:

  • RPL41 functions as a tumor suppressor by maintaining microtubule stability and centrosome integrity.
  • Disruption of RPL41 leads to aberrant mitosis and centrosome dysfunction, contributing to malignant transformation.
  • RPL41 represents a potential therapeutic target in cancers characterized by its down-regulation.

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