Rac2 Specificity in Macrophage Integrin Signaling

Pradip, De; Peng, Xiaodong; Durden, Donald L.

doi:10.1074/jbc.m306491200

Cited by 49Cell Adhesion Molecules ResearchProtein Kinase Regulation and GTPase SignalingCellular Mechanics and Interactions

Rac2 Specificity in Macrophage Integrin Signaling

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Pradip, De, Peng, Xiaodong, Durden, Donald L.·2003·Journal of Biological Chemistry

DOI 10.1074/jbc.m306491200

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Abstract

Herein we report that, despite the similarity of Rac2 to Rac1 (92% amino acid identity), macrophages derived from Rac2-/- mice, which continue to express Rac1, display a marked defect in alphavbeta3/alphavbeta5 and alpha4beta1 integrin-directed migration measured on vitronectin and fibronectin fragments (FN-H296), respectively. In contrast, mouse embryo fibroblasts derived from the Rac2 knockout mice utilize Rac1 for migration via alphavbeta3/alphavbeta5 and alpha4beta1. The genetic reconstitution of bone marrow-derived macrophages (BMM) with Rac2 restores the integrin-dependent migration of Rac2-deficient macrophages on vitronectin (VN) and FN-H296. The levels of GTP-Rac2 generated upon specific integrin engagement in wild type macrophages parallels the phenotypic defect observed in Rac2-deficient macrophages; i.e. FN-H296, alpha4beta1 > VN, alphavbeta3/alphavbeta5 > FN-CH271, alpha5beta1 > intact FN. In a COS7 cell system, the expression of Syk kinase alone is sufficient to convert the alpha4beta1 migration response to Rac2 dependence. Therefore, we present the first evidence that the alpha4beta1 receptor in blood cells has evolved a Syk-Rac2 signaling axis to transmit signals required for integrin-directed migration suggesting that Syk kinase in part encodes myeloid Rac2 specificity in vivo.

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α4β1/αvβ3-induced migration requires Rac2 in macrophages and endothelial cells, and this pathway regulates the postnatal angiogenic response in vivo.
“The current investigation began with our initial observation that the provisional integrins, α4β1/αvβ3 induced migration requires a specific isoform of Rac, Rac2 in macrophages and endothelial cells and that this pathway regulated the postnatal angiogenic response in vivo [1], [2].”
From Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo (2014) · cites this paper as [2]
Syk is necessary and sufficient to convert α4β1 integrin-dependent migration in COS7 cells to Rac2 dependency.
“We transduced a nonmyeloid cell, COS7 which expresses Rac1 and α4β1 but not Rac2 or Syk kinase with Syk and/or Rac2 and were able to determine that Syk was necessary and sufficient to convert α4β1 integrin dependent migration in COS7 cells to Rac2 dependency [2].”
From Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo (2014) · cites this paper as [2]
Specific α4β1 and αvβ3/αvβ5 integrin directed migration in macrophages requires Syk and Rac2.
“Previous work from our laboratory demonstrated that specific α4β1 and αvβ3/αvβ5 integrin directed migration in macrophages requires Syk and Rac2 [2].”
From Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo (2014) · cites this paper as [2]
Rac2 knockout mice display a number of hematopoietic defects mostly in blood cell-specific receptor function or hematopoietic-specific effector mechanisms and in kinase pathway-activated cell survival.
“the Rac2 knockout mice display a number of hematopoietic defects mostly in the context of blood cell-specific receptor function or hematopoietic-specific effector mechanisms and also in kinase pathway-activated cell survival [1], [2], [6], [7], [8].”
From Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo (2014) · cites this paper as [2]
Rac2-/- macrophages show minimal to no migration defect for α5β1 or α2β1.
“3) minimal to no migration defect is seen for α5β1 or α2β1 in Rac2-/- Mθs, respectively [2] (Figure 3A).”
From Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo (2014) · cites this paper as [2]

In the absence of Rac2, macrophages and/or neutrophils display decreased microbial killing.
“Previous findings clearly demonstrate that in the absence of Rac2, macrophages and/or neutrophils display suppressed reactive oxygen species (ROS) production, defective chemotaxis, impaired phagocytosis, and decreased microbial killing [1], [2], [6], [7], [8].”
From Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo (2014) · cites this paper as [2]
In the absence of Rac2, macrophages and/or neutrophils display impaired phagocytosis.
“Previous findings clearly demonstrate that in the absence of Rac2, macrophages and/or neutrophils display suppressed reactive oxygen species (ROS) production, defective chemotaxis, impaired phagocytosis, and decreased microbial killing [1], [2], [6], [7], [8].”
From Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo (2014) · cites this paper as [2]
In the absence of Rac2, macrophages and/or neutrophils display suppressed reactive oxygen species (ROS) production.
“Previous findings clearly demonstrate that in the absence of Rac2, macrophages and/or neutrophils display suppressed reactive oxygen species (ROS) production, defective chemotaxis, impaired phagocytosis, and decreased microbial killing [1], [2], [6], [7], [8].”
From Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo (2014) · cites this paper as [2]
In the absence of Rac2, macrophages and/or neutrophils display defective chemotaxis.
“Previous findings clearly demonstrate that in the absence of Rac2, macrophages and/or neutrophils display suppressed reactive oxygen species (ROS) production, defective chemotaxis, impaired phagocytosis, and decreased microbial killing [1], [2], [6], [7], [8].”
From Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo (2014) · cites this paper as [2]

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Authors: Pradip, D., Peng, X., & Durden, D. L.
Affiliations: Indiana University Indianapolis (US)
Corresponding author: Durden, Donald L.
ORCID: Durden, Donald L.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2003-10
Volume: 278
Issue: 43
Pages: 41661-41669
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m306491200
OpenAlex: W1989409992
Semantic Scholar: e0ac5a9088e22c62254cf8a196e0e435555a0764
Cited by: 49
References: 57
Citations by year: 2026: 1 · 2024: 1 · 2023: 2 · 2022: 3 · 2021: 2 · 2020: 1 · 2019: 3 · 2018: 2 · 2017: 2 · 2016: 2 · 2014: 2 · 2013: 2
FWCI: 1.92
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6206 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Cancer Institute (CA 94233, P01CA081403, CA-81403)
Topics: Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Keywords: Rac2, Rac1, macrophages, integrin signaling, alpha4beta1 integrin, integrin αvβ3, integrin αvβ5, cell migration, vitronectin, fibronectin, Syk, bone marrow-derived macrophages
MeSH terms: Syk Kinase, RAC2 GTP-Binding Protein, Animals, Bone Marrow Cells, Cell Adhesion, Chemotaxis, Enzyme Precursors, Fibronectins, Macrophages, Protein-Tyrosine Kinases, Integrins, Mice, Knockout, Receptors, Vitronectin, Vitronectin, GTP Phosphohydrolases, rac GTP-Binding Proteins, rac1 GTP-Binding Protein, Integrin alpha4beta1, Integrin alphaVbeta3, Intracellular Signaling Peptides and Proteins, Mice

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Rac2 Specificity in Macrophage Integrin Signaling

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