Protein Information

Name leucine aminopeptidase
Synonyms Cytosol aminopeptidase; LAP; LAP 3; LAP3; LAP3 protein; LAPEP; Leucine aminopeptidase; Leucine aminopeptidase 3…

Compound Information

Name jasmonic acid
CAS

Reference List

PubMed Abstract RScore(About this table)
19376935 Fowler JH, Narvaez-Vasquez J, Aromdee DN, Pautot V, Holzer FM, Walling LL: Leucine aminopeptidase regulates defense and wound signaling in tomato downstream of jasmonic acid. Plant Cell. 2009 Apr;21(4):1239-51. Epub 2009 Apr 17.
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9526496 Ruiz-Rivero OJ, Prat S: A -308 deletion of the tomato LAP promoters is able to direct flower-specific and MeJA-induced expression in transgenic plants. Plant Mol Biol. 1998 Mar;36(5):639-48.

Tomato and potato leucine aminopeptidase (LAP) mRNAs are induced in response to mechanical wounding and the wound signal molecules, ABA and jasmonic acid.
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7765119 Herbers K, Prat S, Willmitzer L: Functional analysis of a leucine aminopeptidase from Solanum tuberosum L. Planta. 1994;194(2):230-40.

An increase in steady-state protein that was paralleled by an increase in total LAP activity was observed in leaf extracts after supplying jasmonic acid via the petioles.
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11204785 Pautot V, Holzer FM, Chaufaux J, Walling LL: The induction of tomato leucine aminopeptidase genes (LapA) after Pseudomonas syringae pv. tomato infection is primarily a wound response triggered by coronatine. Mol Plant Microbe Interact. 2001 Feb;14(2):214-24.

Coronatine treatment of excised shoots caused increases in RNAs for jasmonic acid (JA)-regulated wound-response genes (LapA and pin2) but did not influence expression of a JA-regulated pathogenesis-related protein gene (PR-1).
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17896114 Narvaez-Vasquez J, Tu CJ, Park SY, Walling LL: Targeting and localization of wound-inducible leucine aminopeptidase A in tomato leaves. Planta. 2008 Jan;227(2):341-51. Epub 2007 Sep 26.

The localization of LAP-A was distinct from the location of early wound-response proteins that are important in the biosynthesis of jasmonic acid or systemin and more similar to the late wound-response proteins with primary roles in defense.
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1392612 Hildmann T, Ebneth M, Pena-Cortes H, Sanchez-Serrano JJ, Willmitzer L, Prat S: General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding. Plant Cell. 1992 Sep;4(9):1157-70.

Four other wound-induced, ABA-responsive genes that encode two additional proteinase inhibitors, the proteolytic enzyme leucine aminopeptidase, and the biosynthetic enzyme threonine deaminase were isolated from potato plants.
Also, application of methyl jasmonate (MeJA) induced a strong accumulation of these transcripts, both in wild-type and in ABA-deficient plants, thus supporting a role for jasmonic acid as an intermediate in the signaling pathway that leads from ABA accumulation in response to wounding to the transcriptional activation of the genes.
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15231736 Boter M, Ruiz-Rivero O, Abdeen A, Prat S: Conserved MYC transcription factors play a key role in jasmonate signaling both in tomato and Arabidopsis. Genes Dev. 2004 Jul 1;18(13):1577-91.


Jasmonates (JA) are important regulators of plant defense responses that activate expression of many wound-induced genes including the tomato proteinase inhibitor II (pin2) and leucine aminopeptidase (LAP) genes.
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9161035 Dammann C, Rojo E, Sanchez-Serrano JJ: Abscisic acid and jasmonic acid activate wound-inducible genes in potato through separate, organ-specific signal transduction pathways. Plant J. 1997 Apr;11(4):773-82.

When roots of intact plants were treated with JA, high levels of proteinase inhibitor II (pin2), cathepsin D inhibitor, leucine aminopeptidase and threonine deaminase mRNAs accumulated in the systemic leaves.
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10444081 Chao WS, Gu YQ, Pautot V V, Bray EA, Walling LL: Leucine aminopeptidase RNAs, proteins, and activities increase in response to water deficit, salinity, and the wound signals systemin, methyl jasmonate, and abscisic acid . Plant Physiol. 1999 Aug;120(4):979-92.

Comparison of LapA expression with that of the PR-1 (pathogenesis-related 1) and GluB (basic beta-1,3-glucanase) genes indicated that these PR protein genes were modulated by a systemin-independent jasmonic acid-signaling pathway.
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