The Genesis of Tyrosine Phosphorylation

Hunter, Tony

doi:10.1101/cshperspect.a020644

Cited by 141 publications

(137 citation statements)

References 65 publications

(66 reference statements)

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“…They have provided the basis for understanding (1) the requirement for dimerization for kinase activation, and (2) the mechanism of transphosphorylation (Shibuya 2013;Song et al 2013;Barton et al 2014;Hunter 2014). The first crystal structures of the liganded ErbB1 receptor (Garrett et al 2002;Ogiso et al 2002) revealed an extended extracellular structure with ligand binding between domains 1 and 3 and dimerization through domain 2, confirming an earlier model of Lemmon et al (1997) of two EGF:two ErbB1 receptors.…”

Section: What Is the Structure Of The Erbb1 In Living Cells?supporting

confidence: 61%

Structure-Function Relationships of ErbB RTKs in the Plasma Membrane of Living Cells

Arndt‐Jovin¹,

Botelho²,

Jovin³

2014

Cold Spring Harbor Perspectives in Biology

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We review the states of the ErbB family of receptor tyrosine kinases (RTKs), primarily the EGF receptor (EGFR, ErbB1, HER1) and the orphan receptor ErbB2 as they exist in living mammalian cells, focusing on four main aspects: (1) aggregation state and distribution in the plasma membrane; (2) conformational features of the receptors situated in the plasma membrane, compared to the crystallographic structures of the isolated extracellular domains; (3) coupling of receptor disposition on filopodia with the transduction of signaling ligand gradients; and (4) ligand-independent receptor activation by application of a magnetic field.T his review deals exclusively with the disposition and function of the human ErbB (HER) family of receptor tyrosine kinases (RTKs) in the plasma membrane of living cells. We have divided the material into four main topics: (1) distribution and aggregation state of ErbB family members; (2) the 3D structure of the ErbB1 and ErbB2 receptors; (3) the role of receptors located on extensions (filopodia) of the cell body; and (4) the phenomenon and implications of nonligand-dependent activation of the receptors. DISTRIBUTION OF ErbB FAMILY MEMBERS IN THE PLASMA MEMBRANE OF LIVING CELLSThe association state(s) and activities of the ErbB family members in intact living cells differ widely depending on the expression level (number per cell) and the distribution (density, state of homo-and heteroassociation) of each receptor. There are numerous, highly contradictory views about the aggregation state of the receptors in the literature. During the last few years more accurate assessments of receptor distribution have been conducted on living rather than fixed cells. In the latter case, numerous artifacts account for important quantitative discrepancies. One example is the failure of formaldehyde fixation to prevent receptor redistribution (Brock et al. 1999;Tanaka et al. 2010). A more fundamental consideration relates to the hierarchical organization of the plasma membrane, extensively investigated and most recently reviewed by Kusumi et al. (2011). These investigators propose the existence of (1) a mesoscale (40 -300 nm) compartmentalization with actin cytoskeletal "fences" and transmembrane protein "pickets," (2) lipid raft domains (2 -

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Section: What Is the Structure Of The Erbb1 In Living Cells?supporting

confidence: 61%

Structure-Function Relationships of ErbB RTKs in the Plasma Membrane of Living Cells

Arndt‐Jovin¹,

Botelho²,

Jovin³

2014

Cold Spring Harbor Perspectives in Biology

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“…This latter group is of special interest in the context of signal transduction, as exemplified by the pTyr-interacting Src homology 2 (SH2) domains [66,67]. In fact one of the most important functions of phosphotyrosine (pTyr) is to act as a docking site that mediates specific interactions between the phosphoprotein and another protein (or region of the same protein) that contains a pTyr-binding domain, such as SH2 or phosphotyrosine binding (PTB) (for review [68,69]). As far as pSer/pThr is concerned the first binding proteins to be identified were the so called 14-3-3 proteins [70], which tightly regulate G2-M progression through a series of interactions with the mitotic regulatory tyrosine phosphatase Cdc25 [71,72].…”

Section: Phosphotyrosine Comes Into the Scenementioning

confidence: 99%

From phosphoproteins to phosphoproteomes: a historical account

2017

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The first phosphoprotein (casein) was discovered in 1883, yet the enzyme responsible for its phosphorylation was identified only 130 years later, in 2012. In the intervening time, especially in the last decades of the 1900s, it became evident that, far from being an oddity, phosphorylation affects the majority of eukaryotic proteins during their lifespan, and that this reaction is catalysed by the members of a large family of protein kinases, susceptible to a variety of stimuli controlling nearly every aspect of life and death. The aim of this review is to present a historical account of the main steps of this spectacular revolution, which transformed our conception of a biochemical reaction originally held as a sporadic curiosity into the master mechanism governing cell regulation, and, if it is perturbed, causing cell dysregulation.

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“…[80][81][82] If one embraces Julian's idea of antibiotics as mediators of cell-cell communication, it is interesting also to consider aminoglycoside phosphotransferases potentially serving as modulators of such signaling pathways-much as kinases that act on key regulatory proteins can profoundly alter cellular and developmental signaling networks. [83][84][85][86] Julian's challenge to us, to rethink just what roles antibiotics may play in Nature, illustrates yet once again his creativity, his clarity of thought, his biochemical and evolutionary insights, and why it was such an immense pleasure and privilege to work with him in Geneva and Madison some four decades ago.…”

Section: Aminoglycosides Sequence Relationships Of Their Phosphotranmentioning

confidence: 99%

Julian Davies and the discovery of kanamycin resistance transposon Tn5

Berg

2016

J Antibiot

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This paper recounts some of my fond memories of a collaboration between Julian Davies and myself that started in 1974 in Geneva and that led to our serendipitous discovery of the bacterial kanamycin resistance transposon Tn5, and aspects of the lasting positive impact of our interaction and discovery on me and the community. Tn5 was one of the first antibiotic resistance transposons to be found. Its analysis over the ensuing decades provided valuable insights into mechanisms and control of transposition, and led to its use as a much-valued tool in diverse areas of molecular genetics, as also will be discussed here. The Journal of Antibiotics (2017) 70, 339-346; doi:10.1038/ja.2016.120; published online 12 October 2016 BACKGROUND It was wonderfully educational, productive and exciting for me to work with Julian Davies for a few years in the mid 1970s, doing experiments that led to the serendipitous discovery and initial characterizations of kanamycin resistance transposon Tn5 1 -one of the first and most useful of the many bacterial antibiotic resistance (AR) transposons that have been found. 2 I was inspired by Julian's knowledge of mechanisms of antibiotic action and resistance mechanisms, his creativity and clarity of thought and expression, as illustrated in his numerous papers, 3-6 and by his high energy, kindness and inventive good humor-traits that have enriched the lives and careers of many people over the years. Described here, in tribute to Julian and his special character, are my memories of a collaboration that led to Tn5's unexpected discovery, Tn5's properties, and some lasting impacts of our collaboration on the field and on me personally.We began interacting in 1974, soon after Julian arrived in Geneva to begin his sabbatical with Pierre Francois Spahr (Department of Molecular Biology of the University). 7 I was then in my fourth (final) year as Chargé de Recherche (senior postdoc) in Lucien Caro's group in the same department, studying λdv plasmids, often in collaboration with Grete Kellenberger-Gujer, also in Lucien's group 8-13 -and during these years, also hugely enjoying features in and out of the lab that have drawn researchers to Geneva for decades: a superb scientific atmosphere, year-round easy access to the exquisite Alps and Jura mountains, and the language, cuisine and culture of Geneva and vicinity. I had become intrigued the year before by Julian's ideas about origins and evolution of resistance genes, as described in his paper with Raoul Benveniste. 14 They advanced the then-novel theory that the types of bacteria that had provided life saving antibiotics were also the ancestral sources of AR genes that were becoming increasingly common in human and veterinary pathogens. Their inferences were

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The Genesis of Tyrosine Phosphorylation

Cited by 141 publications

References 65 publications

Structure-Function Relationships of ErbB RTKs in the Plasma Membrane of Living Cells

Structure-Function Relationships of ErbB RTKs in the Plasma Membrane of Living Cells

From phosphoproteins to phosphoproteomes: a historical account

Julian Davies and the discovery of kanamycin resistance transposon Tn5

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