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Citation for Study 25352

Citation title: "SUMO Protease SMT7 Modulates Ribosomal Protein L30 and Regulates Cell-size Checkpoint Function".

Study name: "SUMO Protease SMT7 Modulates Ribosomal Protein L30 and Regulates Cell-size Checkpoint Function".

This study is part of submission 25352 (Status: Published).

Citation

Lin Y., Fang S., Chung C., Chen M., & Chen C. 2020. SUMO Protease SMT7 Modulates Ribosomal Protein L30 and Regulates Cell-size Checkpoint Function. The Plant Cell, .

Authors

• Lin Y. (submitter) +88665056630#212
• Fang S.
• Chung C.
• Chen M.
• Chen C.

Abstract

Proliferating cells actively coordinate growth and cell division to ensure cell-size homeostasis; however, the underlying mechanism through which size is controlled is poorly understood. Defect in a SUMO protease protein, SMT7, has been shown to reduce cell division number and increase cell size of the small-size mutant mating type locus 3-4 (mat3-4), which contains a defective Chlamydomonas retinoblastoma tumor suppressor-related protein. Here we describe development of an in vitro SUMOylation system using Chlamydomonas components and use it to provide evidence that SMT7 is a bona fide SUMO protease. We further demonstrate that the SUMO protease activity is required for supernumerous mitotic divisions of the mat3-4 cells. In addition, we identified ribosomal protein L30 (RPL30) as a prime SMT7 target and demonstrated that its SUMOylation is an important modulator of cell division in mat3-4 cells. Loss of SMT7 caused elevated SUMOylated RPL30 levels. Importantly, overexpression of the translational fusion version of RPL30-SUMO4, which mimics elevation of the SUMOylated RPL30 protein in mat3-4, caused a decrease in mitotic division and recapitulated the size-increasing phenotype of the smt7-1 mat3-4 cells. In summary, our study reveals a novel mechanism through which a SUMO protease regulates cell division in the mat3-4 mutant of Chlamydomonas and provides yet another important example of the role that protein SUMOylation can play in regulating key cellular processes, including cell division.

Keywords

Chlamydomonas reinhardtii, SUMO protease, cell cycle, cell size, ribosomal protein

External links

• DOI: 10.1105/tpc.19.00301
• Other URL: http://purl.org/phylo/treebase/phylows/study/TB2:S25352

About this resource

• Canonical resource URI: http://purl.org/phylo/treebase/phylows/study/TB2:S25352
• Other versions: Nexus NeXML
• Show BibTeX reference

  		@ARTICLE{TreeBASE2Ref30177,
  	 author = {Yen-Ling  Lin and Su-Chiung  Fang and  Chin-Lin  Chung and Ming-Hui  Chen and  Chun-Han  Chen},
  	 title = {SUMO Protease SMT7 Modulates Ribosomal Protein L30 and Regulates Cell-size Checkpoint Function},
  	 year = {2020},
  	 keywords = {Chlamydomonas reinhardtii, SUMO protease, cell cycle, cell size, ribosomal protein},
  	 doi = {10.1105/tpc.19.00301},
  	 url = {http://purl.org/phylo/treebase/phylows/study/TB2:S25352},
  	 pmid = {},
  	 journal = {The Plant Cell},
  	 volume = {},
  	 number = {},
  	 pages = {},
  	 abstract = {  Proliferating cells actively coordinate growth and cell division to ensure cell-size homeostasis; however, the underlying mechanism through which size is controlled is poorly understood. Defect in a SUMO protease protein, SMT7, has been shown to reduce cell division number and increase cell size of the small-size mutant mating type locus 3-4 (mat3-4), which contains a defective Chlamydomonas retinoblastoma tumor suppressor-related protein. Here we describe development of an in vitro SUMOylation system using Chlamydomonas components and use it to provide evidence that SMT7 is a bona fide SUMO protease. We further demonstrate that the SUMO protease activity is required for supernumerous mitotic divisions of the mat3-4 cells. In addition, we identified ribosomal protein L30 (RPL30) as a prime SMT7 target and demonstrated that its SUMOylation is an important modulator of cell division in mat3-4 cells. Loss of SMT7 caused elevated SUMOylated RPL30 levels. Importantly, overexpression of the translational fusion version of RPL30-SUMO4, which mimics elevation of the SUMOylated RPL30 protein in mat3-4, caused a decrease in mitotic division and recapitulated the size-increasing phenotype of the smt7-1 mat3-4 cells. In summary, our study reveals a novel mechanism through which a SUMO protease regulates cell division in the mat3-4 mutant of Chlamydomonas and provides yet another important example of the role that protein SUMOylation can play in regulating key cellular processes, including cell division.}
  }
  		

• Show RIS reference

  		TY  - JOUR
  ID  - 30177
  AU  - Lin,Yen-Ling 
  AU  - Fang,Su-Chiung 
  AU  - Chung, Chin-Lin 
  AU  - Chen,Ming-Hui 
  AU  - Chen, Chun-Han 
  T1  - SUMO Protease SMT7 Modulates Ribosomal Protein L30 and Regulates Cell-size Checkpoint Function
  PY  - 2020
  KW  - Chlamydomonas reinhardtii
  KW  - SUMO protease
  KW  - cell cycle
  KW  - cell size
  KW  - ribosomal protein
  UR  - http://purl.org/phylo/treebase/phylows/study/TB2:S25352
  N2  -   Proliferating cells actively coordinate growth and cell division to ensure cell-size homeostasis; however, the underlying mechanism through which size is controlled is poorly understood. Defect in a SUMO protease protein, SMT7, has been shown to reduce cell division number and increase cell size of the small-size mutant mating type locus 3-4 (mat3-4), which contains a defective Chlamydomonas retinoblastoma tumor suppressor-related protein. Here we describe development of an in vitro SUMOylation system using Chlamydomonas components and use it to provide evidence that SMT7 is a bona fide SUMO protease. We further demonstrate that the SUMO protease activity is required for supernumerous mitotic divisions of the mat3-4 cells. In addition, we identified ribosomal protein L30 (RPL30) as a prime SMT7 target and demonstrated that its SUMOylation is an important modulator of cell division in mat3-4 cells. Loss of SMT7 caused elevated SUMOylated RPL30 levels. Importantly, overexpression of the translational fusion version of RPL30-SUMO4, which mimics elevation of the SUMOylated RPL30 protein in mat3-4, caused a decrease in mitotic division and recapitulated the size-increasing phenotype of the smt7-1 mat3-4 cells. In summary, our study reveals a novel mechanism through which a SUMO protease regulates cell division in the mat3-4 mutant of Chlamydomonas and provides yet another important example of the role that protein SUMOylation can play in regulating key cellular processes, including cell division.
  L3  - 10.1105/tpc.19.00301
  JF  - The Plant Cell
  VL  - 
  IS  - 
  ER  -