Initial characterization of TREM-like transcript (TLT)–1: a putative inhibitory receptor within the TREM cluster

The TREMs (triggering receptors expressed on myeloid cells) represent a family of 5 receptors clustered on murine chromosome 17. TREMs 1 and 2 affect various aspects of myeloid cell activation and development, including responsiveness to lipopolysaccharide and regulation of dendritic cell maturation, yet no inhibitory receptor has been demonstrated within this cluster. Here we characterize TLT-1 (TREM-like transcript-1), a putative inhibitory receptor within the TREM cluster that contains an extracellular V-set Ig domain, a proline-rich region, and an immune receptor tyrosine-based inhibitory motif (ITIM) in its cytoplasmic tail. To our knowledge, TLT-1 is the first ITIM-containing receptor carrying a potential Src homology 3 domain ligand. TLT-1 transcripts are abundant in bone marrow cells, but not in lymphocytes, and phosphorylated TLT-1 associates with SHP-1, suggesting that it is indeed an inhibitory receptor. Based on these characteristics, it is likely that TLT-1 regulates the signaling of the TREM family receptors.

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Identification and characterization of SPRK, a novel src-homology 3 domain-containing proline-rich kinase with serine/threonine kinase activity.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)36578-x ◽

1994 ◽

Vol 269 (21) ◽

pp. 15092-15100 ◽

Cited By ~ 4

Author(s):

K.A. Gallo ◽

M.R. Mark ◽

D.T. Scadden ◽

Z. Wang ◽

Q. Gu ◽

...

Keyword(s):

Kinase Activity ◽

Serine Threonine Kinase ◽

Threonine Kinase ◽

Src Homology 3 ◽

Src Homology 3 Domain ◽

Src Homology ◽

Identification And Characterization

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Characterization of the Mouse Src Homology 3 Domain GeneSh3d2con Chr 7 Demonstrates Coexpression with Huntingtin in the Brain and Identifies the Processed PseudogeneSh3d2c-ps1on Chr 2

Genomics ◽

10.1006/geno.1998.5584 ◽

1998 ◽

Vol 54 (3) ◽

pp. 505-510 ◽

Cited By ~ 5

Author(s):

U. Zechner ◽

S. Scheel ◽

M. Hemberger ◽

M. Hopp ◽

T. Haaf ◽

...

Keyword(s):

Src Homology 3 ◽

Src Homology 3 Domain ◽

Src Homology ◽

The Brain

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Site-selective characterization of Src homology 3 domain molecular recognition with cyanophenylalanine infrared probes

Analytical Methods ◽

10.1039/c5ay00523j ◽

2015 ◽

Vol 7 (17) ◽

pp. 7234-7241 ◽

Cited By ~ 11

Author(s):

Rachel E. Horness ◽

Edward J. Basom ◽

Megan C. Thielges

Keyword(s):

Ir Spectroscopy ◽

Src Homology 3 ◽

Src Homology 3 Domain ◽

Src Homology ◽

Ft Ir ◽

Site Selective ◽

Infrared Probes ◽

Ft Ir Spectroscopy ◽

Present Site

We present site-selective CNPhe labeling combined with FT IR spectroscopy as a fast, minimally-perturbative, reproducible approach to characterize protein microenvironments.

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Structure-based characterization of the binding of peptide to the human endophilin-1 Src homology 3 domain using position-dependent noncovalent potential analysis

Journal of Molecular Modeling ◽

10.1007/s00894-011-1197-y ◽

2011 ◽

Vol 18 (5) ◽

pp. 2153-2161 ◽

Cited By ~ 5

Author(s):

Chunjiang Fu ◽

Gang Wu ◽

Fenglin Lv ◽

Feifei Tian

Keyword(s):

Potential Analysis ◽

Src Homology 3 ◽

Src Homology 3 Domain ◽

Src Homology

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Faculty Opinions recommendation of The Src homology 3 domain of the beta-subunit of voltage-gated calcium channels promotes endocytosis via dynamin interaction.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1064854.517791 ◽

2007 ◽

Author(s):

Brett Adams

Keyword(s):

Calcium Channels ◽

Beta Subunit ◽

Voltage Gated ◽

Src Homology 3 ◽

Voltage Gated Calcium Channels ◽

Src Homology 3 Domain ◽

Src Homology

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Faculty Opinions recommendation of Identification of a link between the SAMP repeats of adenomatous polyposis coli tumor suppressor and the Src homology 3 domain of DDEF.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1141847.598934 ◽

2009 ◽

Author(s):

Chloe Bulinski ◽

Andy Tran

Keyword(s):

Tumor Suppressor ◽

Adenomatous Polyposis Coli ◽

Adenomatous Polyposis ◽

Polyposis Coli ◽

Src Homology 3 ◽

Src Homology 3 Domain ◽

Src Homology

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Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk

Journal of Biological Chemistry ◽

10.1016/s0021-9258(20)30059-4 ◽

1994 ◽

Vol 269 (52) ◽

pp. 32781-32787

Author(s):

B S Knudsen ◽

S M Feller ◽

H Hanafusa

Keyword(s):

Guanine Nucleotide Exchange Factor ◽

Guanine Nucleotide ◽

Nucleotide Exchange ◽

Exchange Factor ◽

Src Homology 3 ◽

Guanine Nucleotide Exchange ◽

Nucleotide Exchange Factor ◽

Src Homology 3 Domain ◽

Src Homology ◽

Unique Specificity

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Myosin 1E coordinates actin assembly and cargo trafficking during clathrin-mediated endocytosis

Molecular Biology of the Cell ◽

10.1091/mbc.e11-04-0383 ◽

2012 ◽

Vol 23 (15) ◽

pp. 2891-2904 ◽

Cited By ~ 57

Author(s):

Jackie Cheng ◽

Alexandre Grassart ◽

David G. Drubin

Keyword(s):

Mammalian Cells ◽

Actin Polymerization ◽

Type I ◽

Actin Assembly ◽

Significant Delay ◽

Src Homology 3 ◽

Integral Role ◽

Src Homology 3 Domain ◽

Src Homology ◽

Endocytic Vesicles

Myosin 1E (Myo1E) is recruited to sites of clathrin-mediated endocytosis coincident with a burst of actin assembly. The recruitment dynamics and lifetime of Myo1E are similar to those of tagged actin polymerization regulatory proteins. Like inhibition of actin assembly, depletion of Myo1E causes reduced transferrin endocytosis and a significant delay in transferrin trafficking to perinuclear compartments, demonstrating an integral role for Myo1E in these actin-mediated steps. Mistargeting of GFP-Myo1E or its src-homology 3 domain to mitochondria results in appearance of WIP, WIRE, N-WASP, and actin filaments at the mitochondria, providing evidence for Myo1E's role in actin assembly regulation. These results suggest for mammalian cells, similar to budding yeast, interdependence in the recruitment of type I myosins, WIP/WIRE, and N-WASP to endocytic sites for Arp2/3 complex activation to assemble F-actin as endocytic vesicles are being formed.

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