Protein targeting of an unusual, evolutionarily conserved adenylate kinase to a eukaryotic flagellum

Timothy J. Pullen, Michael L. Ginger, Simon J. Gaskell, Keith Gull

Research output: Contribution to journalArticlepeer-review

61 Citations (Scopus)


The eukaryotic flagellum is a large structure into which specific constituent proteins must be targeted, transported and assembled after their synthesis in the cytoplasm. Using Trypanosoma brucei and a proteomic approach, we have identified and characterized a novel set of adenylate kinase proteins that are localized to the flagellum. These proteins represent unique isoforms that are targeted to the flagellum by an N-terminal extension to the protein and are incorporated into an extraaxonemal structure (the paraflagellar rod). We show that the N-terminal extension is both necessary for isoform location in the flagellum and sufficient for targeting of a green fluorescent protein reporter protein to the flagellum. Moreover, these N-terminal extension sequences are conserved in evolution and we find that they allow the identification of novel adenylate kinases in the genomes of humans and worms. Given the existence of specific isoforms of certain central metabolic enzymes, and targeting sequences for these isoforms, we suggest that these isoforms form part of a complex, "solid-phase" metabolic capability that is built into the eukaryotic flagellum.

Original languageEnglish
Pages (from-to)3257-3265
Number of pages9
JournalMolecular Biology of the Cell
Issue number7
Early online date14 May 2004
Publication statusPublished - 1 Jul 2004
Externally publishedYes


Dive into the research topics of 'Protein targeting of an unusual, evolutionarily conserved adenylate kinase to a eukaryotic flagellum'. Together they form a unique fingerprint.

Cite this