his.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Mal and MyD88: adapter proteins involved in signal transduction by Toll-like receptors
Department of Biochemistry, Trinity College Dublin, Ireland.
Department of Biochemistry, Trinity College Dublin, Ireland.
Department of Biochemistry, Trinity College Dublin, Ireland.ORCID iD: 0000-0002-3053-4543
Department of Biochemistry, Trinity College Dublin, Ireland.
Show others and affiliations
2003 (English)In: Journal of Endotoxin Research, ISSN 0968-0519, E-ISSN 1743-2839, Vol. 9, no 1, 55-59 p.Article in journal (Refereed) Published
Abstract [en]

Signal transduction processes activated by Toll-like receptors (TLRs) include the important transcription factor NF-kappaB and 2 MAP kinases, p38 and Jun N-terminal kinase. These signals ultimately give rise to increased expression of a multitude of pro-inflammatory proteins. Receptor-proximal proteins involved in signalling by all TLRs include the adapter MyD88, 3 IRAKs (IRAK-4, IRAK and IRAK-2), Tollip, Traf-6 and TAK-1. Differences between signals generated by TLRs are emerging, with both TLR4 and TLR2 signalling requiring an additional adapter termed MyD88-adapter-like (Mal; also known as TIRAP). MyD88 and Mal both have a homologous Toll/IL-1 receptor (TIR) domain although they differ in their N-termini, with MyD88 possessing a death domain. In addition, structural models reveal marked differences in surface charges which, when taken with surface charge differences between TLR2 and TLR4 TIR domains, may indicate that TLR4 but not TLR2 recruits Mal directly. Another difference is that Mal can become phosphorylated. Future studies on Mal will reveal specificities in signal transduction by different TLRs, which may ultimately provide molecular explanations for specificities in the innate immune response to infection.

Place, publisher, year, edition, pages
Maney Publishing, 2003. Vol. 9, no 1, 55-59 p.
National Category
Biochemistry and Molecular Biology
Research subject
Natural sciences; Medical sciences
Identifiers
URN: urn:nbn:se:his:diva-9893DOI: 10.1177/09680519030090010701ISI: 000181702400007PubMedID: 12691620ScopusID: 2-s2.0-0037226672OAI: oai:DiVA.org:his-9893DiVA: diva2:743764
Conference
7th Biennial Conference of the International-Endotoxin-Society, Arlington, Virginia, July 18-21, 2002
Available from: 2014-09-05 Created: 2014-09-05 Last updated: 2015-01-07Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMedScopus

Search in DiVA

By author/editor
Ejdebäck, Mikael
In the same journal
Journal of Endotoxin Research
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 1158 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf