Journal article
Arg188 drives RhoC membrane binding
Small GTPases, Vol.8(2), pp.114-121
04/03/2017
DOI: 10.1080/21541248.2016.1205334
PMCID: PMC5464120
PMID: 27355867
Abstract
RhoA and RhoC GTPases are 92% identical but demonstrate unique regulation and function. Phosphorylation of Ser188 has widely been reported to inhibit RhoA activity. RhoC possesses Arg188 in place of Ser188 but retains a canonical upstream PKA recognition sequence. We report here that RhoC-R188S was a PKA substrate in vitro and exhibited less GTP loading compared to wild-type RhoC when expressed in cells. Transiently expressed RhoC was found to be significantly more membrane associated than RhoA. Membrane association of RhoC-R188S and RhoC-R188A were similar to each other and wild-type RhoA, suggesting that Arg188 directly promotes RhoC membrane binding. The positive influence of Arg188 on RhoC membrane association was evident in a constitutively active (Q63L) background. In accordance, RhoA-S188R was significantly more membrane associated than either RhoA or RhoA-S188A. Altogether, these data suggest that swapping residue 188 identity effectively flips the membrane binding profile of wild-type RhoA and RhoC through positive arginine contribution rather than negative phosphoserine regulation.
Details
- Title: Subtitle
- Arg188 drives RhoC membrane binding
- Creators
- Aditi Patel - Wartburg CollegeSophia Williams-Perez - Wartburg CollegeNicole Peyton - Wartburg CollegeAmy Reicks - Wartburg CollegeJustin Buzick - Wartburg CollegeJanean Farley - Wartburg CollegeSarah Shirar - Wartburg CollegeShawn M. Ellerbroek - Wartburg College
- Resource Type
- Journal article
- Publication Details
- Small GTPases, Vol.8(2), pp.114-121
- DOI
- 10.1080/21541248.2016.1205334
- PMID
- 27355867
- PMCID
- PMC5464120
- NLM abbreviation
- Small GTPases
- ISSN
- 2154-1248
- eISSN
- 2154-1256
- Publisher
- Taylor & Francis
- Number of pages
- 8
- Language
- English
- Date published
- 04/03/2017
- Academic Unit
- Pathology
- Record Identifier
- 9984966846302771
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