STK31 is a cell-cycle regulated protein that contributes to the tumorigenicity of epithelial cancer cells

PLoS One. 2014 Mar 25;9(3):e93303. doi: 10.1371/journal.pone.0093303. eCollection 2014.

Abstract

Serine/threonine kinase 31 (STK31) is one of the novel cancer/testis antigens for which its biological functions remain largely unclear. Here, we demonstrate that STK31 is overexpressed in many human colorectal cancer cell lines and tissues. STK31 co-localizes with pericentrin in the centrosomal region throughout all phases of the cell cycle. Interestingly, when cells undergo mitosis, STK31 also localizes to the centromeres, central spindle, and midbody. This localization behavior is similar to that of chromosomal passenger proteins, which are known to be the important players of the spindle assembly checkpoint. The expression of STK31 is cell cycle-dependent through the regulation of a putative D-box near its C-terminal region. Ectopically-expressed STK31-GFP increases cell migration and invasive ability without altering the proliferation rate of cancer cells, whereas the knockdown expression of endogenous STK31 by lentivirus-derived shRNA results in microtubule assembly defects that prolong the duration of mitosis and lead to apoptosis. Taken together, our results suggest that the aberrant expression of STK31 contributes to tumorigenicity in somatic cancer cells. STK31 might therefore act as a potential therapeutic target in human somatic cancers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carcinogenesis*
  • Cell Cycle*
  • Cell Line, Tumor
  • Cell Movement
  • Centrosome / metabolism
  • Colorectal Neoplasms / pathology
  • Gene Expression Regulation, Neoplastic
  • Gene Knockdown Techniques
  • Humans
  • Kinetochores / metabolism
  • Microtubules / metabolism
  • Mitosis
  • Neoplasm Invasiveness
  • Neoplasms, Glandular and Epithelial / pathology*
  • Protein Serine-Threonine Kinases / deficiency
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*
  • Protein Transport
  • RNA, Small Interfering / genetics

Substances

  • RNA, Small Interfering
  • Protein Serine-Threonine Kinases
  • STK31 protein, human

Grants and funding

This work was supported by grants NSC101-2325-B-006-001 and NSC102-2325-B-006-001 from the National Science Council, grant IBMS-CRC100-P01 from Academia Sinica, Project of Promoting Academic Excellence and Developing World Class Research Centers, and the Center for Infectious Disease and Signaling Transduction Research, National Cheng Kung University. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.