Evolution of protein kinase signaling from yeast to man

Manning, Gerard; Plowman, Gregory D.; Hunter, Tony; Sudarsanam, Sucha

doi:10.1016/s0968-0004(02)02179-5

Cited by 871 publications

(714 citation statements)

References 52 publications

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“…Most of the kinase families found in the genome of Homo sapiens are also present in other metazoans such as yeast, worm and fly. Human kinases are, however, twice as many as in the fly or worms [12]. The higher complexity of the human kinome is accounted for by expansion of families whose members control processes that are more developed in higher metazoans, such as haematopoiesis, angiogenesis and immunity [12].…”

Section: Protein Kinase Phylogeny and Structurementioning

confidence: 99%

“…Human kinases are, however, twice as many as in the fly or worms [12]. The higher complexity of the human kinome is accounted for by expansion of families whose members control processes that are more developed in higher metazoans, such as haematopoiesis, angiogenesis and immunity [12]. About 10% of all ePKs were found to lack key residues involved with catalysis.…”

Section: Protein Kinase Phylogeny and Structurementioning

confidence: 99%

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Protein kinases controlling the onset of mitosis

Ferrari

2006

Cell. Mol. Life Sci.

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Abstract. This review article focuses on protein kinases regulating the onset and transition through mitosis. The essay begins by introducing the structural features of the protein kinase catalytic domain and emphasizing the mechanism of enzymatic activation of this class of proteins. Next follows a short historical perspective on cell division and a description of our current understanding of mitosis. In the central part of the review I examine the four major kinases that set the stage for mitosis, which

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Section: Protein Kinase Phylogeny and Structurementioning

confidence: 99%

Section: Protein Kinase Phylogeny and Structurementioning

confidence: 99%

Protein kinases controlling the onset of mitosis

Ferrari

2006

Cell. Mol. Life Sci.

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“…Signaling events have been considered to act through cell surface receptors to transduce cytosolic signals via the actions of tyrosine and serine/threonine kinases, or by eliciting 'second messengers' such as Ca þ 2 and cAMP. [1][2][3] However, a relatively new concept termed 'dependence' has been applied to a growing number of receptors. 4 Dependence receptors, generally, maintain the capacity to elicit cell signaling events similar to the 'classic' receptors, but also maintain a capacity to signal 'negatively' in the absence of their cognate ligand.…”

Section: Introductionmentioning

confidence: 99%

Integrins as a distinct subtype of dependence receptors

Stupack

2005

Cell Death Differ

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In the absence of their cognate ligand, dependence receptors trigger programmed cell death. This function is the defining feature of dependence receptors, which include members of several different protein families. The integrins are a family of heterodimeric receptors for extracellular matrix (ECM) proteins, mediating cell anchorage and migration. Integrins share characteristics with dependence receptors, and integrin binding to substrate ECM ligands is essential for cell survival. Although integrins do not conform in all characteristics to the established definitions of dependence receptors, alterations in the expression of integrins and their ligands during physiological and pathological events, such as wound healing, angiogenesis and tumorigenesis, do regulate cell fate in a ligand-dependent manner. This biosensory function of integrins fits well with our current concept of dependence receptor action, and thus integrins may rightly be considered to comprise a distinct subclass of dependence receptor.

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“…Protein kinase C (121) is known for its multiple functions in the cellular process 21) . Although the function of this protein in silkworms is not clear, it must play an important role in fat cells because the protein (131) that has the Src homology 2 motif was uniquely found in FBs proteome.…”

Section: Protein Identification and Expressionmentioning

confidence: 99%

Proteome analysis of silkworm 1. Fat body

et al. 2009

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SUMMARYProteome analysis of silkworm (Bombyx mori L.) fat bodies was performed on the fifthinstar day-3 larva stage and the expression of proteins separated on two-dimensional polyacrylamide gels was tracked from the fourth-instar day-1 larva stage to the stage before adult moth. Proteins on the 2D-gels were excised manually and treated with 4-vinylpyridine for alkylation. Each spot was analyzed by capillary high-performance liquid chromatography coupled with ion-trap mass spectrometry after proteolysis using trypsin. In the previous report 1) , the amino acid sequence database obtained from the Drosophila genome was used for the protein identification. This analysis used the amino acid sequence data elucidated from the silkworm genome. Additionally, protein expression in fat bodies was compared with that at other stages and in other tissues described in the silkworm proteome database (http://kaiko2ddb.dna.affrc.go.jp/cgi-bin/search_2DDB.cgi). Several unidentified proteins from the previous report 1) were identified with high Mascot scores. Induction and reduction of proteins during metamorphosis were observed as changes in spot concentration on sequential 2D-gels on the web.

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Evolution of protein kinase signaling from yeast to man

Cited by 871 publications

References 52 publications

Protein kinases controlling the onset of mitosis

Protein kinases controlling the onset of mitosis

Integrins as a distinct subtype of dependence receptors

Proteome analysis of silkworm 1. Fat body

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