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Interacting partners of Rac1 (P29S/Q61L) compared to constitutively active Rac1 (Q61L)

ABSTRACT: Interactors of double mutant Rac1 (P29S/Q61L) compared to constitutively active Rac1 (Q61L).

INSTRUMENT(S): Q Exactive

ORGANISM(S): Chlorocebus Sabaeus

TISSUE(S): Fibroblast, Cell Line Cell

DISEASE(S): Disease Free

SUBMITTER: Sergio Lilla

LAB HEAD: Sara Rossana Zanivan

PROVIDER: PXD013941 | Pride | 2019-11-12

REPOSITORIES: Pride

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			Action	DRS
	20180525_SEL_HF_SA_JAW_R02_100518_GFP_r01_001.raw	Raw
	20180525_SEL_HF_SA_JAW_R02_100518_GFP_r02_002.raw	Raw
	20180525_SEL_HF_SA_JAW_R02_100518_GFP_r03_003.raw	Raw
	20180525_SEL_HF_SA_JAW_R02_100518_Rac1-P29S-Q61L_r01_D_007.raw	Raw
	20180525_SEL_HF_SA_JAW_R02_100518_Rac1-P29S-Q61L_r02_D_008.raw	Raw

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Publications

CYRI/ Fam49 Proteins Represent a New Class of Rac1 Interactors.

Whitelaw Jamie A JA Lilla Sergio S Paul Nikki R NR Fort Loic L Zanivan Sara S Machesky Laura M LM

Communicative & integrative biology 20190723 1

Fam49 proteins, now referred to as CYRI (CYFIP-related Rac Interactor), are evolutionarily conserved across many phyla. Their closest relative by amino acid sequence is CYFIP, as both proteins contain a domain of unknown function DUF1394. We recently showed that CYRI and the DUF1394 can mediate binding to Rac1 and evidence is building to suggest that CYRI plays important roles in cell migration, chemotaxis and pathogen entry into cells. Here we discuss how CYRI proteins fit into the current fram ...[more]

PMID: 31413787

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Silcening RAC1 expression suppresses the proliferation of colon cancer cells by inducing gene differentially expressed.

Project description:In this study,RAC1 expression was silenced by RNA interference in colon cancer cell lines, and investigate the correlation between RAC1 expression and colon cancer proliferation,and differential expressed genes were analized by gene assay and qPCR technologe.The proliferation and colony formation ability of colon cancer cells were significantly reduced after RAC1 knockdown. More 1200 known genes were found to be involved in the RAC1 functions related tumorigenesis by genechip analysis, these genes related to cell proliferation/apoptosis and cell cycle process. qRT-PCR results showed an expression pattern consistent with that of the genechip analysis. Lentivirus-mediated RNA interference was used to knockdown RAC1 expression in colon cancer cell lines. And cell proliferation assays . GeneChip analysis were carried out for mRNA expression profiling, followed, the expressed levels of mRNA and protein were measured by Quantitative real-time polymerase chain reaction (qRT-PCR) and western blot, respectively.

2016-02-20 | E-GEOD-78093 | biostudies-arrayexpress

Local GTP availability is an essential step in regulation of RAC1 activity and cell invasion

Project description:Physiological changes in GTP levels in live cells have never been considered a regulatory step of RAC1 activation because GTP concentrations determined by chromatography or mass spectrometry were shown to be substantially higher than the RAC1 GTP dissociation constant (RAC1-GTP Kd) determined in vitro. Here, using a combination of genetically engineered intracellular GTP sensors, recently generated by us, and RAC1 activity reporter, we demonstrate that fluctuations in GTP levels within the range of RAC1-GTP Kd, correlate with changes in RAC1 activity in live cells. We further demonstrate that RAC1 co-localize in protrusions of invading cells with the de novo guanylate biosynthesis enzymes including rate-limiting inosine monophosphate dehydrogenase 2 (IMPDH2) and guanosine monophosphate synthase (GMPS). This colocalization is partly driven by direct interaction of RAC1 with the Bateman domain of IMPDH2. Substitution of endogenous IMPDH2 with the IMPDH2 mutants incapable of binding RAC1 did not affect total intracellular GTP levels but suppressed RAC1 activity. Accordingly, targeting of IMPDH2 away from the plasma membrane did not alter total intracellular GTP pools but decreased local GTP levels in cell protrusions, downregulated RAC1 activity and decreased cell invasion. These data provide previously unrecognized mechanistic insight into the regulation of RAC1 activity by local GTP pools in live cells.

2021-11-04 | PXD028540 | Pride

DNA microarray analysis using murine cerebellum at P6

Project description:We analysed genes upregulated or down regulated by double deletion of Rac1 and Rac3 (Rac1/Rac3-DKO) in cerebellar granule neurons compared with control, using the external granule layer (EGL) dissected from Rac1/Rac3-DKO cerebellum at P6. Rac1-KO mouse is an inducible knockout, in which Rac1 is specifically deleted in cerebellar granule neurons under control of Atoh1 (also called Math1) promoter. In contrast, Rac3-KO mouse is a conventional/simple KO, in which Rac3 is deleted in all cells in the body. Total RNA from the medial portion of the EGL of Rac1/Rac3-DKO and control cerebella at P6 was extracted using TRIzol (Invitrogen). The quality and quantity of RNA were determined using the Agilent 2100 BioAnalyzer.

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Fam49/CYRI interacts with Rac1 and locally suppresses protrusions

Project description:Actin-based protrusions driving cell migration are reinforced through positive feedback, but it is unclear how the cell restricts the eventual size of protrusions, or limits positive signals to allow them to split or retract. We have identified an evolutionarily conserved regulator of the protrusion machinery, which we name CYRI (CYFIP-related Rac interactor). CYRI binds specifically to activated Rac1 via a common motif that is also found in CYFIP, the Domain of Unknown Function DUF1394; we demonstrate that DUF1394 as a new class of Rac1 binding module. CYRI-depleted cells have broad, Scar/WAVE-enriched lamellipodia and display an enhanced duration and extent of pseudopod extension in response to optogenetic Rac1 activation. Conversely, CYRI overexpression suppresses recruitment of active Scar/WAVE complex to the cell edge and results in short-lived, unproductive protrusions. CYRI dynamically inhibits Scar/WAVE induced actin to focus positive protrusion signals and regulate pseudopod complexity. It therefore behaves like a “local inhibitor” predicted and described in widely accepted mathematical models, but not previously identified in living cells. CYRI is important for processes requiring polarity and plasticity of protrusions, including directional chemotactic migration and polarization of epithelial cysts.

2018-10-08 | PXD010460 | Pride

Transcriptome of K14 V12 Rac1 mice

Project description:Wholeskin from transgenic mice overexpressing epidermal specific (K14) activated mutant (V12) Rac1 analyzed with Illumina MouseRef8 v2 Gene Expression arrays Three V12 Rac1 7 day old pups compared to three 7 day old litter-mate controls

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Effect of Rac1 haploinsufficiency on the gene expression profile of mouse endothelial cells

Project description:The therapeutic potential of neurotrophic factors has been hampered by their inability to achieve adequate tissue penetration. Brain blood vessels, however, could be an alternative target for neuro-salvage therapies by virtue of their close proximity to neurons. Here we show that hemizygous deletion of Rac1 in mouse endothelial cells (ECs) attenuates brain injury and edema following focal cerebral ischemia. To explore the mechanisms whereby decrease of Rac1 in ECs provide neuroprotection, ECs were derived from Rac1+/+ and Rac1+/- mice. Microarray analysis was performed to determine the differential gene expression between Rac1+/+ and Rac1+/- ECs. Rac1+/+ and Rac1+/- ECs were cultured to subconfluence. Total RNA was extracted and reverse transcribed. Rac1+/+ (n = 2) and Rac1+/- (n = 2) EC cDNAs were labeled with Cy3 and Cy5, respectively, and equimolar mixtures of labeled Rac1+/+ and Rac1+/- probes were hybridized to 2 slides (sample #21648, #21649). Additionally, Rac1+/+ (n = 2) and Rac1+/- (n=2) EC cDNAs labeled with Cy5 and Cy3 (dye-swapping) were hybridized to 2 slides (sample #21650, #21651). Comparison of signal intensities between Rac1+/+ (channel 2) and Rac1+/- (channel 1) was conducted on each slide (sample), and the ratio of intensities from 4 slides were statistically assessed for each gene feature to investigate differential gene expression.

2009-03-15 | E-GEOD-15003 | biostudies-arrayexpress

Pseudomonas sp. RAC1

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Transcription profiling of rac1 knock-down zebrafish embryos

Project description:Phenotypic, proteome and transcriptome analysis of rac1 knockdown in zebrafish embryos

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Structural mechanisms of autoinhibition and substrate recognition by the ubiquitin ligase HACE1

Project description:Ubiquitin ligases (E3s) are pivotal specificity determinants in the ubiquitin system by selecting substrates and decorating them with distinct ubiquitin signals. Structure determination of the underlying, specific E3-substrate complexes, however, has proven challenging due to their transient nature. In particular, it is incompletely understood how members of the catalytic cysteine-driven class of HECT-type ligases position substrate proteins for modification. Here we report a cryo-EM structure of the full-length human HECT-type ligase HACE1, along with solution-based conformational analyses by small-angle X-ray scattering and hydrogen-deuterium exchange mass spectrometry. Structure-based functional analyses in vitro and in cells reveal that the activity of HACE1 is stringently regulated by dimerization-induced autoinhibition. The inhibition occurs at the first step of the catalytic cycle and is thus substrate-independent. We employ mechanism-based chemical crosslinking to reconstitute a complex of activated, monomeric HACE1 with its major substrate, RAC1, visualize its structure by cryo-EM, and validate the binding mode by solution-based analyses. Our findings explain how HACE1 achieves selectivity in ubiquitinating the active, GTP-loaded state of RAC1 and establish a framework for interpreting mutational alterations of the HACE1-RAC1 interplay in disease. More broadly, this work illuminates central unexplored aspects in the architecture, conformational dynamics, regulation, and specificity of full-length HECT-type ligases.

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Effect of Rac1 haploinsufficiency on the gene expression profile of mouse endothelial cells

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