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Updated: Feb 11, 2026

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Splicing variant of Cdc42 interacting protein-4 disrupts beta-catenin-mediated cell-cell adhesion: expression and

Emiko Tsuji1, Yuji Tsuji, Toshiyuki Fujiwara

  • 1Tenjin Tsuji Clinic, Fukuoka, Japan. emikot@tt-clinic.com

Biochemical and Biophysical Research Communications
|December 14, 2005
PubMed

Insights

A novel variant of Cdc42-interacting protein 4 (CIP4) was found in kidney cancer (RCC) patients, causing loss of cell adhesion and promoting cancer spread. This CIP4 variant disrupts cell-cell connections, potentially driving RCC metastasis.

Area of Science:

  • Molecular Biology
  • Oncology
  • Cell Biology

Background:

  • Renal cell carcinoma (RCC) is a significant health concern with complex molecular underpinnings.
  • Cdc42-interacting protein 4 (CIP4) plays roles in cellular processes, but its specific involvement in RCC is not fully understood.

Purpose of the Study:

  • To identify and characterize alternative splicing variants of CIP4 in renal cell carcinoma.
  • To investigate the functional consequences of a novel CIP4 variant (CIP4-V) on cell adhesion and beta-catenin signaling in RCC.

Main Methods:

  • Sequence analysis and reverse transcription-PCR were used to identify the CIP4 splicing variant.
  • Functional assays were performed to assess the impact of CIP4-V overexpression on cell morphology, cell-cell adhesion, and protein localization.

Main Results:

  • An aberrant splicing event in the CIP4 gene, resulting in the CIP4-V variant, was identified in nearly 50% of RCC samples.
  • CIP4-V encodes a truncated protein lacking key functional domains and leads to the formation of ubiquitinated aggresomes.
  • Overexpression of CIP4-V causes loss of cell-cell adhesion by increasing beta-catenin tyrosine phosphorylation and promoting its mistrafficking.

Conclusions:

  • CIP4 is crucial for maintaining beta-catenin-mediated cell-cell adhesion.
  • The identified CIP4-V variant contributes to RCC pathogenesis by disrupting cell adhesion, potentially promoting metastasis and invasiveness.

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