The Linker for Activation of B Cells (LAB)/Non-T Cell Activation Linker (NTAL) Regulates Triggering Receptor Expressed on Myeloid Cells (TREM)-2 Signaling and Macrophage Inflammatory Responses Independently of the Linker for Activation of T Cells
Open accessAbstract
Triggering receptor expressed on myeloid cells-2 (TREM-2) is rapidly emerging as a key regulator of the innate immune response via its regulation of macrophage inflammatory responses. Here we demonstrate that proximal TREM-2 signaling parallels other DAP12-based receptor systems in its use of Syk and Src-family kinases. However, we find that the linker for activation of T cells (LAT) is severely reduced as monocytes differentiate into macrophages and that TREM-2 exclusively uses the linker for activation of B cells (LAB encoded by the gene Lat2(-/-)) to mediate downstream signaling. LAB is required for TREM-2-mediated activation of Erk1/2 and dampens proximal TREM-2 signals through a novel LAT-independent mechanism resulting in macrophages with proinflammatory properties. Thus, Lat2(-/-) macrophages have increased TREM-2-induced proximal phosphorylation, and lipopolysaccharide stimulation of these cells leads to increased interleukin-10 (IL-10) and decreased IL-12p40 production relative to wild type cells. Together these data identify LAB as a critical, LAT-independent regulator of TREM-2 signaling and macrophage development capable of controlling subsequent inflammatory responses.
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In the context of microglia, the kinase responsible for phosphorylating the ITAM residues on DAP12 is likely to be Src or a Src-family kinase such as Lyn.
“In the context of microglia, the kinase responsible for phosphorylating the Immunoreceptor Tyrosine Activation Motif (ITAM) residues on DAP12 is likely to be Src [62] or a Src-family kinase such as Lyn [63, 64].”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [62]
Within microglia it has been suggested that LAT, LAB or LAT2, rather than BLNK, could be phosphorylated by Syk, or that Syk may directly phosphorylate and activate PLCγ2, thus bypassing BTK.
“Within microglia it has been suggested that Linkers for Activation of T- and B-cells (LAT, LAB or LAT2), rather than BLNK, could be phosphorylated by Syk, or that Syk may directly phosphorylate and activate PLCγ2, thus bypassing BTK in these cells [4, 62].”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [62]
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- Authors
- Whittaker, G. C., Orr, S. J., Quigley, L., Hughes, L., Francischetti, I. M. B., Zhang, W., & McVicar, D. W.
- Affiliations
- National Institutes of Health (US)
- Duke Medical Center (US)
- Corresponding author
- McVicar, Daniel W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-01
- Volume
- 285
- Issue
- 5
- Pages
- 2976-2985
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2823438
- OpenAlex
- W2101132430
- Cited by
- 33
- References
- 41
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 3 · 2019: 2 · 2018: 1 · 2017: 3 · 2016: 3 · 2014: 4 · 2013: 3 · 2012: 3
- FWCI
- 1.00
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- ORCA Online Research @Cardiff (Cardiff University) (submittedVersion)
- Research Portal (Queen's University Belfast) (submittedVersion)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (R01AI048674, R01AI056156)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Inflammation biomarkers and pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
- Keywords
- TREM2, LAT, LAT2, macrophage inflammation, DAP12, Syk, Src family kinases, ERK1/2 phosphorylation, monocyte differentiation, IL-10, IL-12, innate immunity, receptor signaling
- MeSH terms
- Animals, B-Lymphocytes, Lipopolysaccharides, Lymphocyte Activation, Macrophages, Membrane Glycoproteins, Membrane Proteins, Mice, Inbred C57BL, Phosphoproteins, Receptors, Immunologic, T-Lymphocytes, Signal Transduction, Interleukin-10, Amino Acid Transport System y+, Fusion Regulatory Protein 1, Light Chains, Adaptor Proteins, Signal Transducing, Mice, GRB2 Adaptor Protein, Interleukin-12 Subunit p40
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