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Review
. 2021 Dec 20:8:804166.
doi: 10.3389/fmed.2021.804166. eCollection 2021.

TRIM29 in Cutaneous Squamous Cell Carcinoma

Che-Yuan Hsu  1 , Teruki Yanagi  1 , Hideyuki Ujiie  1
Affiliations
Review

TRIM29 in Cutaneous Squamous Cell Carcinoma

Che-Yuan Hsu et al. Front Med (Lausanne). .

Abstract

Tripartite motif (TRIM) proteins play important roles in a wide range of cell physiological processes, such as signal transduction, transcriptional regulation, innate immunity, and programmed cell death. TRIM29 protein, encoded by the ATDC gene, belongs to the RING-less group of TRIM protein family members. It consists of four zinc finger motifs in a B-box domain and a coiled-coil domain, and makes use of the B-box domain as E3 ubiquitin ligase in place of the RING. TRIM29 was found to be involved in the formation of homodimers and heterodimers in relation to DNA binding; additional studies have also demonstrated its role in carcinogenesis, DNA damage signaling, and the suppression of radiosensitivity. Recently, we reported that TRIM29 interacts with keratins and FAM83H to regulate keratin distribution. Further, in cutaneous SCC, the expression of TRIM29 is silenced by DNA methylation, leading to the loss of TRIM29 and promotion of keratinocyte migration. This paper reviews the role of TRIM family proteins in malignant tumors, especially the role of TRIM29 in cutaneous SCC.

Keywords: ATDC; FAM83H; TRIM29; cell migration; keratin; squamous cell carcinoma.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
The domains of TRIM29 and FAM83H interact with keratin in cutaneous squamous cell carcinoma. (A) TRIM29 is pertinent to RING-less group of TRIM family proteins, which consist of four zinc finger motifs in the B-box domain and a coiled-coil domain. The zinc finger, B-box, coiled-coil, and C-terminal domains of TRIM29 are all essential for the construction of the TRIM29–keratin–FAM83H complex. (B) FAM83 members have a common N-terminal domain (domain unknown function 1669: DUF1669) and a C-terminal domain. The C-terminal domain of FAM83H is required for the formation of the TRIM29–keratin–FAM83H complex.
Figure 2
Figure 2
TRIM29 can act as either an oncogene or a tumor suppressor depending on the tumor type.
Figure 3
Figure 3
TRIM29 was proven to colocalize with keratin 5, keratin 14, and FAM83H in the cytosol, and to form the TRIM29–keratin–FAM83H complex. FAM83H and TRIM29 can be characterized as sharing similar features in regulating keratin distribution and cell migration. The TRIM29–keratin–FAM83H complex is thought to regulate the keratin distribution in cutaneous SCC.
See this image and copyright information in PMC

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