PROSITE documentation PDOC51860REM-1 domain profile
Rho GTPases are molecular switches that regulate many essential cellular processes, including actin dynamics, gene transcription, cell-cycle progression and cell adhesion. In the GTP-bound form they are able to interact with effector or target molecules to initiate a downstream response, while an intrinsic GTPase activity returns the proteins to the GDP-bound state, to complete the cycle and terminate signal transduction. The Rho effector motif class 1 (REM-1) domain specifically binds GTP-Rho and is widely conserved in the following Rho effector proteins [1,2,3]:
- Vertebrate serine/threonine-protein kinases N (PKNs), contain three copies of the REM-1 domain. Many proteins that interact with PKNs are involved with the cytoskeletal network, e.g. α-actinin and vimentin. PKNs are also implicated in the control of transcrption factors, mitogenesis, and cell regulation. PKNs have also been shown to play a role in apoptosis and to be involved in keratinocyte cell-cell adhesion with increased PKN activity promoting cell-cell adhesion [4,5].
- Vertebrate PKN-related proteins (Rhophilins, RHPNs).
- Vertebrate Rhotekins (RTKNs).
- Animal transducer of Cdc42-dependent actin assembly (TOCA) family proteins, comprise an N-terminal F-BAR domain (see <PDOC51741>), a central REM-1 domain, and a C-terminal SH3 domain (see <PDOC50002>) [6].
- Yeast protein kinase C-like 1 (PKC1).
The REM-1 domain contains two long α helices forming a left-handed antiparallel coiled-coil fold (see <PDB:5FRG>) termed the antiparallel coiled-coil (ACC) finger domain. The two long helices encompass the basic region and the leucine repeat region, which are identified as the Rho-binding region [4,5,6].
The profile we developed covers the entire REM-1 domain.
Last update:March 2018 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Watanabe G. Saito Y. Madaule P. Ishizaki T. Fujisawa K. Morii N. Mukai H. Ono Y. Kakizuka A. Narumiya S. |
| Title | Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho. | |
| Source | Science 271:645-648(1996). | |
| PubMed ID | 8571126 |
| 2 | Authors | Reid T. Furuyashiki T. Ishizaki T. Watanabe G. Watanabe N. Fujisawa K. Morii N. Madaule P. Narumiya S. |
| Title | Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain. | |
| Source | J. Biol. Chem. 271:13556-13560(1996). | |
| PubMed ID | 8662891 |
| 3 | Authors | Bishop A.L. Hall A. |
| Title | Rho GTPases and their effector proteins. | |
| Source | Biochem. J. 348:241-255(2000). | |
| PubMed ID | 10816416 |
| 4 | Authors | Maesaki R. Ihara K. Shimizu T. Kuroda S. Kaibuchi K. Hakoshima T. |
| Title | The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1. | |
| Source | Mol. Cell 4:793-803(1999). | |
| PubMed ID | 10619026 |
| 5 | Authors | Owen D. Lowe P.N. Nietlispach D. Brosnan C.E. Chirgadze D.Y. Parker P.J. Blundell T.L. Mott H.R. |
| Title | Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1). | |
| Source | J. Biol. Chem. 278:50578-50587(2003). | |
| PubMed ID | 14514689 | |
| DOI | 10.1074/jbc.M304313200 |
| 6 | Authors | Watson J.R. Fox H.M. Nietlispach D. Gallop J.L. Owen D. Mott H.R. |
| Title | Investigation of the Interaction between Cdc42 and Its Effector TOCA1: HANDOVER OF Cdc42 TO THE ACTIN REGULATOR N-WASP IS FACILITATED BY DIFFERENTIAL BINDING AFFINITIES. | |
| Source | J. Biol. Chem. 291:13875-13890(2016). | |
| PubMed ID | 27129201 | |
| DOI | 10.1074/jbc.M116.724294 |
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