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Article ; Online: Cellular responses to extracellular guidance cues.

Berzat, Anastacia / Hall, Alan

2010 Volume 29, Issue 16, Page(s) 2734–2745

Abstract: Extracellular guidance cues have a key role in orchestrating cell behaviour. They can take many forms, including soluble and cell-bound ligands (proteins, lipids, peptides or small molecules) and insoluble matrix substrates, but to act as guidance cues, ... ...

Abstract	Extracellular guidance cues have a key role in orchestrating cell behaviour. They can take many forms, including soluble and cell-bound ligands (proteins, lipids, peptides or small molecules) and insoluble matrix substrates, but to act as guidance cues, they must be presented to the cell in a spatially restricted manner. Cells that recognize such cues respond by activating intracellular signal transduction pathways in a spatially restricted manner and convert the extracellular information into intracellular polarity. Although extracellular cues influence a broad range of cell polarity decisions, such as mitotic spindle orientation during asymmetric cell division, or the establishment of apical-basal polarity in epithelia, this review will focus specifically on guidance cues that promote cell migration (chemotaxis), or localized cell shape changes (chemotropism).
MeSH term(s)	Animals ; Cell Shape ; Chemotaxis ; Humans ; Signal Transduction
Language	English
Publishing date	2010-08-18
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.1038/emboj.2010.170
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Article ; Online: Regulation of the Rho family small GTPase Wrch-1/RhoU by C-terminal tyrosine phosphorylation requires Src.

Alan, Jamie K / Berzat, Anastacia C / Dewar, Brian J / Graves, Lee M / Cox, Adrienne D

Molecular and cellular biology

2010 Volume 30, Issue 17, Page(s) 4324–4338

Abstract: Wrch-1 is an atypical Rho family small GTPase with roles in migration, epithelial cell morphogenesis, osteoclastogenesis, and oncogenic transformation. Here, we observed rapid relocalization of Wrch-1 from the plasma membrane upon serum stimulation. ... ...

Abstract	Wrch-1 is an atypical Rho family small GTPase with roles in migration, epithelial cell morphogenesis, osteoclastogenesis, and oncogenic transformation. Here, we observed rapid relocalization of Wrch-1 from the plasma membrane upon serum stimulation. Studies revealed a requirement for serum-stimulated tyrosine phosphorylation of Wrch-1 at residue Y254 within its C-terminal membrane targeting domain, mediated by the nonreceptor tyrosine kinase Src. Genetic or pharmacological loss of Src kinase activity blocked both phosphorylation and relocalization of Wrch-1. Functionally, Y254 was required for proper Wrch-1 modulation of cystogenesis in three-dimensional culture, and the phospho-deficient mutant, Y254F, was enhanced in Wrch-1-mediated anchorage-independent growth. Mechanistically, C-terminal tyrosine phosphorylation and subsequent relocalization of Wrch-1 downregulated its ability to interact with and activate its effectors by decreasing active Wrch-1-GTP, perhaps by altering proximity to a GEF or GAP. Phospho-deficient Wrch-1(Y254F) remained at the plasma membrane and GTP bound and continued to recruit and activate its effector PAK, even upon serum stimulation. In contrast, a phospho-mimetic mutant, Y254E, was constitutively endosomally localized and GDP bound and failed to recruit PAK unless mutated to be constitutively active/GAP insensitive. C-terminal tyrosine phosphorylation thus represents a new paradigm in posttranslational control of small GTPase localization, activation, and biological function.
MeSH term(s)	Animals ; Cell Line ; Cell Membrane/metabolism ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Phosphorylation ; Protein Transport ; Serum/metabolism ; Tyrosine/metabolism ; p21-Activated Kinases/metabolism ; rho GTP-Binding Proteins/metabolism ; src-Family Kinases/metabolism
Chemical Substances	Tyrosine (42HK56048U) ; Guanosine Triphosphate (86-01-1) ; src-Family Kinases (EC 2.7.10.2) ; p21-Activated Kinases (EC 2.7.11.1) ; RHOU protein, human (EC 3.6.1.-) ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2010-06-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.01646-09
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Article: Using inhibitors of prenylation to block localization and transforming activity.

Berzat, Anastacia C / Brady, Donita C / Fiordalisi, James J / Cox, Adrienne D

Methods in enzymology

2006 Volume 407, Page(s) 575–597

Abstract: The proper subcellular localization and biological activity of most Ras and Rho family small GTPases are dependent on their posttranslational modification by isoprenylation. Farnesyltransferase (FTase) and geranylgeranyl transferase I (GGTase I) are the ... ...

Abstract	The proper subcellular localization and biological activity of most Ras and Rho family small GTPases are dependent on their posttranslational modification by isoprenylation. Farnesyltransferase (FTase) and geranylgeranyl transferase I (GGTase I) are the prenyltransferases that catalyze the irreversible attachment of C15 farnesyl (Ras, Rnd) or C20 (R-Ras, Ral, Rap, Rho, Rac, Cdc42) isoprenoid lipid moieties to these small GTPases and other proteins. Therefore, pharmacological inhibitors of FTase (FTIs) and GGTase I (GGTIs) have been developed to prevent these modifications and thereby to block the lipid-mediated association of Ras and Rho proteins with cellular membranes and the consequent signaling and transforming activities. In addition, other small molecule inhibitors such as farnesyl thiosalicylic acid (FTS) can compete with the isoprenoid moiety of small GTPases for membrane binding sites. Finally, endogenous regulatory proteins such as RhoGDIs can bind to and mask the prenyl groups of small GTPases, leading to their sequestration from membranes. We describe here methods to use each of these categories of prenylation inhibitors to manipulate and investigate the subcellular localization patterns and transforming potential of these Ras and Rho family GTPases.
MeSH term(s)	Alkyl and Aryl Transferases/antagonists & inhibitors ; Animals ; Dimethylallyltranstransferase/antagonists & inhibitors ; Enzyme Inhibitors/pharmacology ; Farnesol/analogs & derivatives ; Farnesol/pharmacology ; Farnesyltranstransferase/antagonists & inhibitors ; GTP Phosphohydrolases/antagonists & inhibitors ; Guanine Nucleotide Dissociation Inhibitors/pharmacology ; Mice ; NIH 3T3 Cells ; Prenylation/drug effects ; Protein Transport/drug effects ; Salicylates/pharmacology ; ras Proteins/antagonists & inhibitors ; rho GTP-Binding Proteins/antagonists & inhibitors ; rho-Specific Guanine Nucleotide Dissociation Inhibitors
Chemical Substances	Enzyme Inhibitors ; Guanine Nucleotide Dissociation Inhibitors ; Salicylates ; farnesylthiosalicylic acid ; rho-Specific Guanine Nucleotide Dissociation Inhibitors ; Farnesol (4602-84-0) ; Alkyl and Aryl Transferases (EC 2.5.-) ; geranylgeranyltransferase type-I (EC 2.5.1.-) ; Dimethylallyltranstransferase (EC 2.5.1.1) ; Farnesyltranstransferase (EC 2.5.1.29) ; GTP Phosphohydrolases (EC 3.6.1.-) ; ras Proteins (EC 3.6.5.2) ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2006
Publishing country	United States
Document type	Journal Article
ISSN	0076-6879
ISSN	0076-6879
DOI	10.1016/S0076-6879(05)07046-1
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Article: Visual monitoring of post-translational lipid modifications using EGFP-GTPase probes in live cells.

Keller, Patricia J / Fiordalisi, James J / Berzat, Anastacia C / Cox, Adrienne D

Methods (San Diego, Calif.)

2005 Volume 37, Issue 2, Page(s) 131–137

Abstract: Modification of small GTPases by lipids is required for their proper subcellular localization and biological activity. Lipids added post-translationally include both farnesyl and geranylgeranyl isoprenoids and the fatty acid palmitate. Thus, specific ... ...

Abstract	Modification of small GTPases by lipids is required for their proper subcellular localization and biological activity. Lipids added post-translationally include both farnesyl and geranylgeranyl isoprenoids and the fatty acid palmitate. Thus, specific small molecule inhibitors of these processes cause mislocalization of small GTPases and impair their biological activity. Common biochemical methods of determining the lipid modification status or inhibitor sensitivity of small GTPases, such as in vitro prenylation assays, SDS-PAGE mobility shifts or metabolic labeling, although highly useful in their own right, cannot distinguish differences among specific subpopulations of cells, link lipid modification status with other properties of interest, or provide spatio-temporal information. An alternative method takes advantage of the tight link between small GTPase lipid modification and subcellular localization. The innate localization pattern of the enhanced green fluorescent protein, a common epitope tag frequently used in live cell imaging, is altered by fusion to modified but not unmodified small GTPases. We describe here a technique that takes advantage of these properties to monitor post-translational modifications of these proteins in a rapid, visual manner in live cells.
MeSH term(s)	Animals ; GTP Phosphohydrolases/genetics ; GTP Phosphohydrolases/metabolism ; Genes, Reporter ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Lipid Metabolism ; Mice ; Molecular Probes ; NIH 3T3 Cells ; Protein Processing, Post-Translational/physiology ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism
Chemical Substances	Molecular Probes ; Recombinant Fusion Proteins ; enhanced green fluorescent protein ; Green Fluorescent Proteins (147336-22-9) ; GTP Phosphohydrolases (EC 3.6.1.-)
Language	English
Publishing date	2005-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2005.05.023
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Zs.A 3239: Show issues

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Article: Atypical mechanism of regulation of the Wrch-1 Rho family small GTPase.

Shutes, Adam / Berzat, Anastacia C / Cox, Adrienne D / Der, Channing J

Current biology : CB

2004 Volume 14, Issue 22, Page(s) 2052–2056

Abstract: Rho family GTPases are GDP/GTP-regulated molecular switches that regulate signaling pathways controlling diverse cellular processes. Wrch-1 was identified as a Wnt-1 regulated Cdc42 homolog, upregulated by Wnt1 signaling in Wnt1-transformed mouse mammary ...

Abstract	Rho family GTPases are GDP/GTP-regulated molecular switches that regulate signaling pathways controlling diverse cellular processes. Wrch-1 was identified as a Wnt-1 regulated Cdc42 homolog, upregulated by Wnt1 signaling in Wnt1-transformed mouse mammary cells, and was able to promote formation of filopodia and activate the PAK serine/threonine kinase. Wrch-1 shares significant sequence and functional similarity with the Cdc42 small GTPase. However, Wrch-1 possesses a unique N-terminal 46 amino acid sequence extension that contains putative Src homology 3 (SH3) domain-interacting motifs. We determined the contribution of the N terminus to Wrch-1 regulation and activity. We observed that Wrch-1 possesses properties that distinguish it from Cdc42 and other Rho family GTPases. Unlike Cdc42, Wrch-1 possesses an extremely rapid, intrinsic guanine nucleotide exchange activity. Although the N terminus did not influence GTPase or GDP/GTP cycling activity in vitro, N-terminal truncation of Wrch-1 enhanced its ability to interact with and activate PAK and to cause growth transformation. The N terminus associated with the Grb2 SH3 domain-containing adaptor protein, and this association increased the levels of active Wrch-1 in cells. We propose that Grb2 overcomes N-terminal negative regulation to promote Wrch-1 effector interaction. Thus, Wrch-1 exhibits an atypical model of regulation not seen in other Rho family GTPases.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Blotting, Western ; DNA Primers ; Fluorescence Polarization ; GRB2 Adaptor Protein ; Gene Expression Regulation ; Humans ; Immunoprecipitation ; Mice ; NIH 3T3 Cells ; Plasmids/genetics ; Protein Binding ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/metabolism ; Pseudopodia/metabolism ; Signal Transduction/physiology ; rho GTP-Binding Proteins/genetics ; rho GTP-Binding Proteins/metabolism ; src Homology Domains/genetics
Chemical Substances	Adaptor Proteins, Signal Transducing ; DNA Primers ; GRB2 Adaptor Protein ; GRB2 protein, human ; Grb2 protein, mouse ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; RHOU protein, human (EC 3.6.1.-) ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2004-11-23
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2004.11.011
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Article: Biochemical analyses of the Wrch atypical Rho family GTPases.

Shutes, Adam / Berzat, Anastacia C / Chenette, Emily J / Cox, Adrienne D / Der, Channing J

Methods in enzymology

2006 Volume 406, Page(s) 11–26

Abstract: The Rho family of GTPases comprises a major branch of the Ras superfamily of small GTPases. To date, at least 22 human members have been identified. However, most of our knowledge of Rho GTPase function comes from the study of the three classical Rho ... ...

Abstract	The Rho family of GTPases comprises a major branch of the Ras superfamily of small GTPases. To date, at least 22 human members have been identified. However, most of our knowledge of Rho GTPase function comes from the study of the three classical Rho GTPases, RhoA, Rac1, and Cdc42. These Rho GTPases function as GDP/GTP-related binary switches that are activated by diverse extracellular signal-mediated stimuli. The activated GTPases then interact with downstream effectors to regulate cytoplasmic signaling networks that in turn regulate actin organization, cell cycle progression, and gene expression. Recently, studies have begun to explore the regulation and function of some of the lesser-known members of the Rho GTPase family. Wrch-1 (Wnt-regulated Cdc42 homolog-1) and the closely related Chp (Cdc42 homologous protein)/Wrch-2 protein comprise a distinct branch of the mammalian Rho GTPase family. Although both share significant sequence and functional similarities with Cdc42, Wrch proteins possess additional N- and C-terminal sequences that distinguish them from the classical Rho GTPases (Cdc42, RhoA, and Rac1). We have determined that Wrch-1 and Wrch2 exhibit unusual GDP/GTP binding properties and undergo posttranslational lipid modifications distinct from those of the classical Rho GTPases. In this chapter, we summarize our experimental approaches used to characterize the biochemical properties of these atypical Rho GTPases.
MeSH term(s)	Animals ; Cell Membrane/drug effects ; Cell Membrane/metabolism ; Chromatography, Affinity/methods ; Chromatography, Liquid/methods ; Escherichia coli/metabolism ; GTP Phosphohydrolases/analysis ; GTP-Binding Proteins/analysis ; GTP-Binding Proteins/metabolism ; Glutathione Transferase/genetics ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Histidine/genetics ; Humans ; Mice ; NIH 3T3 Cells ; Neoplasm Proteins/analysis ; Neoplasm Proteins/metabolism ; Oligopeptides/genetics ; Palmitates/pharmacology ; Palmitic Acid/metabolism ; Recombinant Proteins/isolation & purification ; rho GTP-Binding Proteins/analysis ; rho GTP-Binding Proteins/genetics ; rho GTP-Binding Proteins/metabolism
Chemical Substances	His-His-His-His-His-His ; Neoplasm Proteins ; Oligopeptides ; Palmitates ; RHOV protein, human ; Recombinant Proteins ; Guanosine Diphosphate (146-91-8) ; 2-bromopalmitate (18263-25-7) ; Palmitic Acid (2V16EO95H1) ; Histidine (4QD397987E) ; Guanosine Triphosphate (86-01-1) ; Glutathione Transferase (EC 2.5.1.18) ; GTP Phosphohydrolases (EC 3.6.1.-) ; GTP-Binding Proteins (EC 3.6.1.-) ; RHOU protein, human (EC 3.6.1.-) ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2006
Publishing country	United States
Document type	Journal Article ; Review
ISSN	0076-6879
ISSN	0076-6879
DOI	10.1016/S0076-6879(06)06002-2
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Article: Transforming activity of the Rho family GTPase, Wrch-1, a Wnt-regulated Cdc42 homolog, is dependent on a novel carboxyl-terminal palmitoylation motif.

Berzat, Anastacia C / Buss, Janice E / Chenette, Emily J / Weinbaum, Carolyn A / Shutes, Adam / Der, Channing J / Minden, Audrey / Cox, Adrienne D

The Journal of biological chemistry

2005 Volume 280, Issue 38, Page(s) 33055–33065

Abstract: Wrch-1 is a Rho family GTPase that shares strong sequence and functional similarity with Cdc42. Like Cdc42, Wrch-1 can promote anchorage-independent growth transformation. We determined that activated Wrch-1 also promoted anchorage-dependent growth ... ...

Abstract	Wrch-1 is a Rho family GTPase that shares strong sequence and functional similarity with Cdc42. Like Cdc42, Wrch-1 can promote anchorage-independent growth transformation. We determined that activated Wrch-1 also promoted anchorage-dependent growth transformation of NIH 3T3 fibroblasts. Wrch-1 contains a distinct carboxyl-terminal extension not found in Cdc42, suggesting potential differences in subcellular location and function. Consistent with this, we found that Wrch-1 associated extensively with plasma membrane and endosomes, rather than with cytosol and perinuclear membranes like Cdc42. Like Cdc42, Wrch-1 terminates in a CAAX tetrapeptide (where C is cysteine, A is aliphatic amino acid, and X is any amino acid) motif (CCFV), suggesting that Wrch-1 may be prenylated similarly to Cdc42. Most surprisingly, unlike Cdc42, Wrch-1 did not incorporate isoprenoid moieties, and Wrch-1 membrane localization was not altered by inhibitors of protein prenylation. Instead, we showed that Wrch-1 is modified by the fatty acid palmitate, and pharmacologic inhibition of protein palmitoylation caused mislocalization of Wrch-1. Most interestingly, mutation of the second cysteine of the CCFV motif (CCFV > CSFV), but not the first, abrogated both Wrch-1 membrane localization and transformation. These results suggest that Wrch-1 membrane association, subcellular localization, and biological activity are mediated by a novel membrane-targeting mechanism distinct from that of Cdc42 and other isoprenylated Rho family GTPases.
MeSH term(s)	Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Biotin/chemistry ; Blotting, Western ; Cell Adhesion ; Cell Membrane/metabolism ; Cell Proliferation ; Cysteine/chemistry ; Cytosol/metabolism ; Endosomes/metabolism ; Esters/chemistry ; Green Fluorescent Proteins/metabolism ; Mice ; Microscopy, Fluorescence ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; NIH 3T3 Cells ; Palmitic Acid/chemistry ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry ; Sequence Homology, Amino Acid ; Signal Transduction ; Transfection ; cdc42 GTP-Binding Protein/metabolism ; rho GTP-Binding Proteins/metabolism
Chemical Substances	Esters ; Recombinant Proteins ; Green Fluorescent Proteins (147336-22-9) ; Palmitic Acid (2V16EO95H1) ; Biotin (6SO6U10H04) ; RHOU protein, human (EC 3.6.1.-) ; cdc42 GTP-Binding Protein (EC 3.6.5.2) ; rho GTP-Binding Proteins (EC 3.6.5.2) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2005-07-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M507362200
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Article ; Online: Cellular responses to extracellular guidance cues.

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Article ; Online: Regulation of the Rho family small GTPase Wrch-1/RhoU by C-terminal tyrosine phosphorylation requires Src.

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Article: Using inhibitors of prenylation to block localization and transforming activity.

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Article: Visual monitoring of post-translational lipid modifications using EGFP-GTPase probes in live cells.

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Article: Atypical mechanism of regulation of the Wrch-1 Rho family small GTPase.

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Article: Biochemical analyses of the Wrch atypical Rho family GTPases.

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Article: Transforming activity of the Rho family GTPase, Wrch-1, a Wnt-regulated Cdc42 homolog, is dependent on a novel carboxyl-terminal palmitoylation motif.

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