Phosphorylation of Thr654 but not Thr669 within the juxtamembrane domain of the EGF receptor inhibits calmodulin binding

Aifa, Sami; Frikha, Fakher; Miled, Nabil; Johansen, Knut; Lundström, Ingemar; Svensson, Samuel

doi:10.1016/j.bbrc.2006.05.200

Cited by 24 publications

(29 citation statements)

References 19 publications

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“…The phosphorylation and de-phosphorylation of JMD residues often regulates activity of RLKs, impinging on their enzymatic function or their ability to interact with downstream targets (Aifa et al , 2006; Heiss et al , 2006; Thiel and Carpenter, 2007; Chen et al , 2010). In Erf, the JMD contains only one conserved Thr (Thr645) and no conserved Ser or Tyr residues (Fig.…”

Section: Resultsmentioning

confidence: 99%

Identification of critical functional residues of receptor-like kinase ERECTA

Kosentka

Zhang

Simon

et al. 2017

Journal of Experimental Botany

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Section: Resultsmentioning

confidence: 99%

Identification of critical functional residues of receptor-like kinase ERECTA

Kosentka

Zhang

Simon

et al. 2017

Journal of Experimental Botany

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“…Phosphorylation and dephosphorylation of residues in the JM domain of animal and plant RD RLKs plays an important regulatory role in the signal transduction of these proteins (1)(2)(3)(4)(5) GST-XA21K668 protein was incubated with or without the ATPase His-tagged XB24 (His-XB24). The purified GST-XA21K668 protein was subject to LC-MS/MS analysis.…”

Section: Discussionmentioning

confidence: 99%

A Conserved Threonine Residue in the Juxtamembrane Domain of the XA21 Pattern Recognition Receptor Is Critical for Kinase Autophosphorylation and XA21-mediated Immunity

Chen

Chern

Canlas

et al. 2010

Journal of Biological Chemistry

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Receptor-like kinases (RLKs)3 play important roles in many biological processes, including development and immunity responses, in both animals and plants. Most RLKs possess intrinsic protein kinase activity and regulate downstream signaling through phosphorylation and dephosphorylation events (1-5). Kinases are classified as arginine-aspartate (RD) or non-RD kinases. RD kinases carry a conserved arginine (Arg) immediately preceding the catalytic aspartate (Asp) (6). RD kinases are regulated by autophosphorylation of the activation segment, a centrally located loop positioned close to the catalytic center.In contrast to RD kinases, non-RD kinases typically carry a cysteine or glycine in place of the arginine. We have previously reported that non-RD kinases are associated with the control of early signaling events in both plant and animal innate immunity (7). For example, in humans, non-RD kinases associate with proteins belonging to the Toll-like receptor (TLR) family, which contain leucine-rich repeats in the extracellular domain and Toll-interleukin receptor intracellular domains (8). TLRs recognize pathogen-associated molecular patterns at the cell surface and then activate a common signaling pathway through an association with non-RD kinases to induce a core set of defense responses (9). TLR1, TLR3, TLR5, TLR6, TLR7, TLR8, and TLR9 function through the non-RD interleukin-1 receptor-associated kinase (IRAK1), whereas TLR3 and TLR4 function through the non-RD receptor interacting-protein 1 (10). In plants, RLKs demonstrated to function in mediating innate immunity fall into the non-RD class (10) or are associated with non-RD RLKs (11-13). These include the Arabidopsis pattern recognition receptors (PRRs), flagellin sensitive 2 (FLS2) (14) and elongation factor-Tu receptor (15), the rice PRRs, such as XA21 (16), XA26 (17), and Pid2 (or called Pi-d2) (18), the barley PRG1 (resistance to Puccinia graminis f. sp. tritici) (19), and the Arabidposis RD RLK BAK1 that associates with the non-RD RLK FLS2 (11). Unlike RD kinases, non-RD kinases do not autophosphorylate their activation segments (6,10,20). Given the demonstrated importance of the non-RD class of kinases in innate immunity, there is great interest in understanding their mode of action.RLKs contain a juxtamembrane (JM) domain located between the transmembrane and kinase domains. It is now clear that the JM domain can play an important role in regulating the function of kinase. For example, deletion of the JM domain of the epidermal growth factor (ErbB-1) kinase (an RD RLK) results in a severe loss of tyrosine phosphorylation (1). Two conserved tyrosine phosphorylation sites Tyr 605 and Tyr 611 of EphB2 are essential for EphB2 kinase autophosphorylation and biological responses (21,22). Phosphorylation of the JM domain of the type I transforming growth factor-␤ (T␤R-I, an RD RLK) eliminates the binding site for the FKBP12 (12-kDa FK506-binding protein) inhibitor protein, leading to activation of the T␤R-I kinase (23, 24). To date, the role of the

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“…53 It is intriguing to speculate that calpaindependent proteolysis of Fc␥RIIa is regulated, at least in part, by calmodulin binding and/or phosphorylation at 214 Ser and 217 Ser, as postulated for PKC-dependent modulation of epidermal growth factor receptor activity. 43,73 The activation of dual proteolytic pathways may be more broadly relevant to ITAM-dependent regulation in other cells. For For personal use only.…”

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confidence: 99%

Dual ITAM-mediated proteolytic pathways for irreversible inactivation of platelet receptors: de-ITAM-izing FcγRIIa

Gardiner

Karunakaran

Arthur

et al. 2008

Blood

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Collagen binding to glycoprotein VI (GPVI) induces signals critical for platelet activation in thrombosis. Both ligand-induced GPVI signaling through its coassociated Fc-receptor gamma-chain (FcRgamma) immunoreceptor tyrosine-activation motif (ITAM) and the calmodulin inhibitor, W7, dissociate calmodulin from GPVI and induce metalloproteinase-mediated GPVI ectodomain shedding. We investigated whether signaling by another ITAM-bearing receptor on platelets, FcgammaRIIa, also down-regulates GPVI expression. Agonists that signal through FcgammaRIIa, the mAbs VM58 or 14A2, potently induced GPVI shedding, inhibitable by the metalloproteinase inhibitor, GM6001. Unexpectedly, FcgammaRIIa also underwent rapid proteolysis in platelets treated with agonists for FcgammaRIIa (VM58/14A2) or GPVI/FcRgamma (the snake toxin, convulxin), generating an approximate 30-kDa fragment. Immunoprecipitation/pull-down experiments showed that FcgammaRIIa also bound calmodulin and W7 induced FcgammaRIIa cleavage. However, unlike GPVI, the approximate 30-kDa FcgammaRIIa fragment remained platelet associated, and proteolysis was unaffected by GM6001 but was inhibited by a membrane-permeable calpain inhibitor, E64d; consistent with this, micro-calpain cleaved an FcgammaRIIa tail-fusion protein at (222)Lys/(223)Ala and (230)Gly/(231)Arg, upstream of the ITAM domain. These findings suggest simultaneous activation of distinct extracellular (metalloproteinase-mediated) and intracellular (calpain-mediated) proteolytic pathways irreversibly inactivating platelet GPVI/FcRgamma and FcgammaRIIa, respectively. Activation of both pathways was observed with immunoglobulin from patients with heparin-induced thrombocytopenia (HIT), suggesting novel mechanisms for platelet dysfunction by FcgammaRIIa after immunologic insult.

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Phosphorylation of Thr654 but not Thr669 within the juxtamembrane domain of the EGF receptor inhibits calmodulin binding

Cited by 24 publications

References 19 publications

Identification of critical functional residues of receptor-like kinase ERECTA

Identification of critical functional residues of receptor-like kinase ERECTA

A Conserved Threonine Residue in the Juxtamembrane Domain of the XA21 Pattern Recognition Receptor Is Critical for Kinase Autophosphorylation and XA21-mediated Immunity

Dual ITAM-mediated proteolytic pathways for irreversible inactivation of platelet receptors: de-ITAM-izing FcγRIIa

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