TY - JOUR
T1 - TRIM37
T2 - a critical orchestrator of centrosome function
AU - Domínguez-Calvo, Andrés
AU - Gönczy, Pierre
AU - Holland, Andrew J.
AU - Balestra, Fernando R.
N1 - Funding Information:
This work was supported by the American Cancer Society [MBG-19-173-01-MBG]; National Institutes of Health [R01GM114119]; National Institutes of Health [R01GM133897]; Junta de Aandalucía (es) [US-1255532]; Swiss Cancer Research Foundation (ch) [KFS-3388-02-2014]. We are grateful to Gabriela García Rodríguez for critical reading of the manuscript. This work was supported by project US-1255532 from junta de Andalucía. Work on TRIM37 in the lab of PG has been supported by the Swiss Cancer Research Foundation (KFS-3388-02-2014). Work in the Holland laboratory was supported by the National Institutes of Health grants R01GM114119 and R01GM133897, and an American Cancer Society Mission Boost Grant MBG-19-173-01-MBG. ADC was funded with an FPU fellowship from the Spanish Ministry of Science. FRB was supported by the University of Seville through the V PPIT-US program (US-Cabimer, Seville, Spain). CABIMER is supported by the regional government of Andalucia (Junta de Andalucía).
Funding Information:
We are grateful to Gabriela García Rodríguez for critical reading of the manuscript. This work was supported by project US-1255532 from junta de Andalucía. Work on TRIM37 in the lab of PG has been supported by the Swiss Cancer Research Foundation (KFS-3388-02-2014). Work in the Holland laboratory was supported by the National Institutes of Health grants R01GM114119 and R01GM133897, and an American Cancer Society Mission Boost Grant MBG-19-173-01-MBG. ADC was funded with an FPU fellowship from the Spanish Ministry of Science. FRB was supported by the University of Seville through the V PPIT-US program (US-Cabimer, Seville, Spain). CABIMER is supported by the regional government of Andalucia (Junta de Andalucía).
Publisher Copyright:
© 2021 Informa UK Limited, trading as Taylor & Francis Group.
PY - 2021
Y1 - 2021
N2 - Loss of function mutations in the E3 ubiquitin ligase TRIM37 result in MULIBREY nanism, a disease characterized by impaired organ growth and a high propensity to develop different tumor types. Additionally, increased copy number of TRIM37 is a feature of some breast cancers and neuroblastomas. The molecular role played by TRIM37 in such loss and gain of function conditions has been a focus of research in the last decade, which led notably to the identification of critical roles of TRIM37 in centrosome biology. Specifically, deletion of TRIM37 results in the formation of aberrant centrosomal proteins assemblies, including Centrobin-PLK4 assemblies, which can act as extra MTOCs, thus resulting in defective chromosome segregation. Additionally, TRIM37 overexpression targets the centrosomal protein CEP192 for degradation, thereby preventing centrosome maturation and increasing the frequency of mitotic errors. Interestingly, increased TRIM37 protein levels sensitize cells to the PLK4 inhibitor centrinone. In this review, we cover the emerging roles of TRIM37 in centrosome biology and discuss how this knowledge may lead to new therapeutic strategies to target specific cancer cells.
AB - Loss of function mutations in the E3 ubiquitin ligase TRIM37 result in MULIBREY nanism, a disease characterized by impaired organ growth and a high propensity to develop different tumor types. Additionally, increased copy number of TRIM37 is a feature of some breast cancers and neuroblastomas. The molecular role played by TRIM37 in such loss and gain of function conditions has been a focus of research in the last decade, which led notably to the identification of critical roles of TRIM37 in centrosome biology. Specifically, deletion of TRIM37 results in the formation of aberrant centrosomal proteins assemblies, including Centrobin-PLK4 assemblies, which can act as extra MTOCs, thus resulting in defective chromosome segregation. Additionally, TRIM37 overexpression targets the centrosomal protein CEP192 for degradation, thereby preventing centrosome maturation and increasing the frequency of mitotic errors. Interestingly, increased TRIM37 protein levels sensitize cells to the PLK4 inhibitor centrinone. In this review, we cover the emerging roles of TRIM37 in centrosome biology and discuss how this knowledge may lead to new therapeutic strategies to target specific cancer cells.
KW - 17q23
KW - CEP192
KW - Centrobin
KW - PLK4
KW - TRIM37
KW - centrosome
KW - mulibrey nanism
UR - http://www.scopus.com/inward/record.url?scp=85117614923&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85117614923&partnerID=8YFLogxK
U2 - 10.1080/15384101.2021.1988289
DO - 10.1080/15384101.2021.1988289
M3 - Review article
C2 - 34672905
AN - SCOPUS:85117614923
SN - 1538-4101
VL - 20
SP - 2443
EP - 2451
JO - Cell Cycle
JF - Cell Cycle
IS - 23
ER -