| Dark Blue | possible binding sites at amino acid locations 13-20, 60-64, and 118-121 |
| Yellow | beta sheets |
| Cyan | alpha helices |
| Red | potential phosphorylation site for protein activity regulation; serine residue at amino acid 74 |
| PBD | AF-P92978-F1 |
| UniProt | [1] |
Rho-related GTPases from plants, otherwise known as ROPs, are involved in cell polarity through the regulation of cytoskeleton components like actin and microtubules. [1] [2] Unlike mammalian cells, plant cells do not contain heterotrimeric G proteins like Cdc42, Rac, and Rho that are known to regulate cellular polarity. [2]
Structure and Function
ROP proteins are a type of monomeric G proteins found in plants belonging to the Rho family. [1] ROP binding to GTP or GDP determines its activity due to conformational changes within its structure. [1] Within the G-domain of the structure are the G-box motifs G1-5. These motifs are formed during protein folding and are composed of conserved sequences that are responsible for nucleotide and magnesium binding as well as hydrolysis of GTP. [1] Motifs G2 (switch I loop) and G3 (switch II loop) possess distinct conformations depending on GTP binding state. [1] In addition, the G-domain contains a unique and conserved helical domain commonly found in Rho family proteins called αi. [1]
Specific locations within the 3D ROP protein structure, including the amino acids 13-20, 60-64, and 118-121, act as binding sites during protein activity. [3] The serine residue at amino acid 74 has been shown to be a potential protein activity regulation site through phosphorylation. [4]
References
- ^ a b c d e f Ou, Hongxin; Yi, Peishan (13 July 2022). "ROP GTPase-dependent polarity establishment during tip growth in plants". New Phytologist. 236 (1): 49–57. doi: 10.1111/nph.18373. PMID 35832004. S2CID 250529868 – via New Phytologist Foundation.
- ^ a b Fu, Ying; Yang, Zhenbiao (1 December 2001). "Rop GTPase: a master switch of cell polarity development in plants". Trends in Plant Science. 6 (12): 545–547. doi: 10.1016/S1360-1385(01)02130-6. PMID 11738369 – via Cell Press.
- ^ "UniProt". www.uniprot.org. Retrieved 2023-05-04.
- ^ Ménesi, Dalma; Klement, Éva; Ferenc, Györgyi; Fehér, Attila (2021). "The Arabidopsis Rho of Plants GTPase ROP1 Is a Potential Calcium-Dependent Protein Kinase (CDPK) Substrate". Plants. 10 (10) (published 29 September 2021): 2053. doi: 10.3390/plants10102053. ISSN 2223-7747. PMC 8539224. PMID 34685862.
 | This plant physiology article is a stub. You can help Wikipedia by expanding it. |
 | This protein-related article is a stub. You can help Wikipedia by expanding it. |
| Dark Blue | possible binding sites at amino acid locations 13-20, 60-64, and 118-121 |
| Yellow | beta sheets |
| Cyan | alpha helices |
| Red | potential phosphorylation site for protein activity regulation; serine residue at amino acid 74 |
| PBD | AF-P92978-F1 |
| UniProt | [1] |
Rho-related GTPases from plants, otherwise known as ROPs, are involved in cell polarity through the regulation of cytoskeleton components like actin and microtubules. [1] [2] Unlike mammalian cells, plant cells do not contain heterotrimeric G proteins like Cdc42, Rac, and Rho that are known to regulate cellular polarity. [2]
Structure and Function
ROP proteins are a type of monomeric G proteins found in plants belonging to the Rho family. [1] ROP binding to GTP or GDP determines its activity due to conformational changes within its structure. [1] Within the G-domain of the structure are the G-box motifs G1-5. These motifs are formed during protein folding and are composed of conserved sequences that are responsible for nucleotide and magnesium binding as well as hydrolysis of GTP. [1] Motifs G2 (switch I loop) and G3 (switch II loop) possess distinct conformations depending on GTP binding state. [1] In addition, the G-domain contains a unique and conserved helical domain commonly found in Rho family proteins called αi. [1]
Specific locations within the 3D ROP protein structure, including the amino acids 13-20, 60-64, and 118-121, act as binding sites during protein activity. [3] The serine residue at amino acid 74 has been shown to be a potential protein activity regulation site through phosphorylation. [4]
References
- ^ a b c d e f Ou, Hongxin; Yi, Peishan (13 July 2022). "ROP GTPase-dependent polarity establishment during tip growth in plants". New Phytologist. 236 (1): 49–57. doi: 10.1111/nph.18373. PMID 35832004. S2CID 250529868 – via New Phytologist Foundation.
- ^ a b Fu, Ying; Yang, Zhenbiao (1 December 2001). "Rop GTPase: a master switch of cell polarity development in plants". Trends in Plant Science. 6 (12): 545–547. doi: 10.1016/S1360-1385(01)02130-6. PMID 11738369 – via Cell Press.
- ^ "UniProt". www.uniprot.org. Retrieved 2023-05-04.
- ^ Ménesi, Dalma; Klement, Éva; Ferenc, Györgyi; Fehér, Attila (2021). "The Arabidopsis Rho of Plants GTPase ROP1 Is a Potential Calcium-Dependent Protein Kinase (CDPK) Substrate". Plants. 10 (10) (published 29 September 2021): 2053. doi: 10.3390/plants10102053. ISSN 2223-7747. PMC 8539224. PMID 34685862.
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| This plant physiology article is a stub. You can help Wikipedia by expanding it. |
|
| This protein-related article is a stub. You can help Wikipedia by expanding it. |