Home  |  Contact
PROSITE documentation PDOC51860 [for PROSITE entry PS51860]

REM-1 domain profile





Description

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.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Last update:

March 2018 / First entry.

-------------------------------------------------------------------------------

Technical section

PROSITE method (with tools and information) covered by this documentation:

REM_1, PS51860; REM-1 domain profile  (MATRIX)


References

1AuthorsWatanabe G. Saito Y. Madaule P. Ishizaki T. Fujisawa K. Morii N. Mukai H. Ono Y. Kakizuka A. Narumiya S.
TitleProtein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho.
SourceScience 271:645-648(1996).
PubMed ID8571126

2AuthorsReid T. Furuyashiki T. Ishizaki T. Watanabe G. Watanabe N. Fujisawa K. Morii N. Madaule P. Narumiya S.
TitleRhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain.
SourceJ. Biol. Chem. 271:13556-13560(1996).
PubMed ID8662891

3AuthorsBishop A.L. Hall A.
TitleRho GTPases and their effector proteins.
SourceBiochem. J. 348:241-255(2000).
PubMed ID10816416

4AuthorsMaesaki R. Ihara K. Shimizu T. Kuroda S. Kaibuchi K. Hakoshima T.
TitleThe structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1.
SourceMol. Cell 4:793-803(1999).
PubMed ID10619026

5AuthorsOwen D. Lowe P.N. Nietlispach D. Brosnan C.E. Chirgadze D.Y. Parker P.J. Blundell T.L. Mott H.R.
TitleMolecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1).
SourceJ. Biol. Chem. 278:50578-50587(2003).
PubMed ID14514689
DOI10.1074/jbc.M304313200

6AuthorsWatson J.R. Fox H.M. Nietlispach D. Gallop J.L. Owen D. Mott H.R.
TitleInvestigation of the Interaction between Cdc42 and Its Effector TOCA1: HANDOVER OF Cdc42 TO THE ACTIN REGULATOR N-WASP IS FACILITATED BY DIFFERENTIAL BINDING AFFINITIES.
SourceJ. Biol. Chem. 291:13875-13890(2016).
PubMed ID27129201
DOI10.1074/jbc.M116.724294



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)