Contributions of F-BAR and SH2 Domains of Fes Protein Tyrosine Kinase for Coupling to the FcεRI Pathway in Mast Cells

McPherson, Victor; Everingham, Stephanie; Karisch, Robert; Smith, J. A.; Udell, Christian M.; Zheng, Jimin; Jia, Zongchao; Craig, Andrew W.B.

doi:10.1128/mcb.00904-08

Cited by 29 publications

(45 citation statements)

References 74 publications

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“…The FES L145P mutant also showed a similar capacity for binding microtubules (Fig. 4B and C), suggesting this binding is not dependent on the predicted a-helical F-BAR domain of FES (29). It is also worth noting, that incubation of FES 1-459, and not GST or 460-822, caused depolymerisation of microtubules, as evidenced by increased amount of tubulin in the soluble fraction (Fig.…”

Section: Fes Localizes To Microtubules and Promotes Their Organizatiomentioning

confidence: 76%

“…FES has been reported to localize to different cellular compartments, including the nucleus (46,47), plasma membrane (29), the trans-Golgi (48), and localized to microtubules (31,44). These different pools of FES likely signal to distinct substrates involved in cell differentiation, vesicle trafficking, focal adhesions, and cell migration.…”

Section: Discussionmentioning

confidence: 99%

“…Previous results have suggested that FES is constitutively oligomeric, but usually maintained in an inactive state (44). The L145P mutant, designed to be at the center of the first predicted CC domain of FES (45), is located near the tips of the F-BAR dimer generated by homology modeling of the FES F-BAR domain on the structure of FBP17 (29). A detailed characterization of the effects of L145P mutation on F-BAR domain function will be important to fully understand that how FES is regulated by this domain (25).…”

Section: Discussionmentioning

confidence: 99%

“…Glutathione S-transferase fusion protein expression and purification Plasmids encoding glutathione S-transferase (GST) fusions to FES N-terminal (residues 1-459) and C-terminal (460-822) fragments of FES were previously described (29,37). The L145P and R483E mutations were generated in pGEX-FES 1-459 and pGEX-FES 460-822 plasmids using the QuikChange Site-Directed Mutagenesis Kit (Invitrogen) and verified by sequencing.…”

Section: Immunofluorescence Microscopymentioning

confidence: 99%

“…FES, and the related kinase FER, have a unique domain organization among PTKs, including the N-terminal Fer/CIP4 homology-Bin/ Amphiphysin/Rvs (F-BAR), and extended F-BAR (FX) domains, that mediate membrane targeting and oligomerization (28,29). These domains are followed by SH2 and PTK domains that interact with one another to regulate FES kinase activity (30).…”

Section: Introductionmentioning

confidence: 99%

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FES Kinase Promotes Mast Cell Recruitment to Mammary Tumors via the Stem Cell Factor/KIT Receptor Signaling Axis

Kwok

Everingham

Zhang

et al. 2012

Molecular Cancer Research

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KIT receptor is required for mast cell development, survival, and migration toward its ligand stem cell factor (SCF). Many solid tumors express SCF and this leads to mast cell recruitment to tumors and release of mediators linked to tumor angiogenesis, growth, and metastasis. Here, we investigate whether FES protein-tyrosine kinase, a downstream effector of KIT signaling in mast cells, is required for migration of mast cells toward SCF-expressing mammary tumors. Using a novel agarose drop assay for chemotaxis of bone marrow-derived mast cells (BMMC) toward SCF, we found that defects in chemotaxis of fes-null BMMCs correlated with disorganized microtubule networks in polarized cells. FES displayed partial colocalization with microtubules in polarized BMMCs and has at least two direct microtubule binding sites within its N-terminal F-BAR and SH2 domains. An oligomerizationdisrupting mutation within the Fer/CIP4 homology-Bin/Amphiphysin/Rvs (F-BAR) domain had no effect on microtubule binding, whereas microtubule binding to the SH2 domain was dependent on the phosphotyrosinebinding pocket. FES involvement in mast cell recruitment to tumors was tested using the AC2M2 mouse mammary carcinoma model. These tumor cells expressed SCF and promoted BMMC recruitment in a KIT-and FESdependent manner. Engraftment of AC2M2 orthotopic and subcutaneous tumors in control or fes-null mice, revealed a key role for FES in recruitment of mast cells to the tumor periphery. This may contribute to the reduced tumor growth and metastases observed in fes-null mice compared with control mice. Taken together, FES is a potential therapeutic target to limit the progression of tumors with stromal mast cell involvement. Mol Cancer Res; 10(7); 881-91. Ó2012 AACR.

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Section: Fes Localizes To Microtubules and Promotes Their Organizatiomentioning

confidence: 76%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Immunofluorescence Microscopymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

FES Kinase Promotes Mast Cell Recruitment to Mammary Tumors via the Stem Cell Factor/KIT Receptor Signaling Axis

Kwok

Everingham

Zhang

et al. 2012

Molecular Cancer Research

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Receptor‐Free Signaling at Curved Cellular Membranes

Ebrahimkutty

Galic

2019

BioEssays

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Plasma membranes are subject to continuous deformations. Strikingly, some of these transient membrane undulations yield membrane-associated signaling hubs that differ in composition and function, depending on membrane geometry and the availability of co-factors. Here, recent advancements on this ubiquitous type of receptor-independent signaling are reviewed, with a special focus on emerging concepts and technical challenges associated with studying these elusive signaling sites.

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Hematopoietic cell-specific lyn substrate (HCLS1 or HS1): A versatile actin-binding protein in leukocytes

Castro-Ochoa

Guerrero‐Fonseca

Schnoor

2018

Journal of Leukocyte Biology

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Leukocytes are constantly produced in the bone marrow and released into the circulation. Many different leukocyte subpopulations exist that exert distinct functions. Leukocytes are recruited to sites of inflammation and combat the cause of inflammation via many different effector functions. Virtually all of these processes depend on dynamic actin remodeling allowing leukocytes to adhere, migrate, phagocytose, and release granules. However, actin dynamics are not possible without actin‐binding proteins (ABP) that orchestrate the balance between actin polymerization, branching, and depolymerization. The homologue of the ubiquitous ABP cortactin in hematopoietic cells is hematopoietic cell‐specific lyn substrate‐1, often called hematopoietic cell‐specific protein‐1 (HCLS1 or HS1). HS1 has been reported in different leukocytes to regulate Arp2/3‐dependent migration. However, more evidence is emerging that HS1 functions go far beyond just being a direct actin modulator. For example, HS1 is important for the activation of GTPases and integrins, and mediates signaling downstream of many receptors including BCR, TCR, and CXCR4. In this review, we summarize current knowledge on HS1 functions and discuss them in a pathophysiologic context.

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Contributions of F-BAR and SH2 Domains of Fes Protein Tyrosine Kinase for Coupling to the FcεRI Pathway in Mast Cells

Cited by 29 publications

References 74 publications

FES Kinase Promotes Mast Cell Recruitment to Mammary Tumors via the Stem Cell Factor/KIT Receptor Signaling Axis

FES Kinase Promotes Mast Cell Recruitment to Mammary Tumors via the Stem Cell Factor/KIT Receptor Signaling Axis

Receptor‐Free Signaling at Curved Cellular Membranes

Hematopoietic cell-specific lyn substrate (HCLS1 or HS1): A versatile actin-binding protein in leukocytes

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