Kinesin subfamily UNC104 contains a FHA domain: boundaries and physicochemical characterization

A Westerholm-Parvinen, I Vernos, L Serrano

Research output: Contribution to journalArticleScientificpeer-review

24 Citations (Scopus)

Abstract

By sequence analysis we show that the U104 domain found in the UNC104 subfamily of kinesins is a forkhead homology-associated domain (FHA). A combination of limited proteolysis, mass spectroscopy, and physicochemical analysis define this domain as a genuine autonomously folding domain. Our data show that the FHA domain is shorter than previously reported since the C-terminal alpha-helix is not part of its minimum core. Key amino acids postulated to recognize phosphorylated residues are conserved. These data suggest that the kinesin FHA domains are functional domains involved in protein-protein interactions regulated by phosphorylation.

Original languageEnglish
Pages (from-to)285-90
Number of pages6
JournalFEBS Letters
Volume486
Issue number3
DOIs
Publication statusPublished - 15 Dec 2000
MoE publication typeA1 Journal article-refereed

Fingerprint

Kinesin
Proteolysis
Phosphorylation
Sequence Analysis
Mass Spectrometry
Proteins
Spectroscopy
Amino Acids
alpha-Helical Protein Conformation

Keywords

  • Forkhead homology-associated domain
  • Xenopuskinesin-like protein 4
  • Kinesin-like protein
  • UNC104 subfamily

Cite this

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abstract = "By sequence analysis we show that the U104 domain found in the UNC104 subfamily of kinesins is a forkhead homology-associated domain (FHA). A combination of limited proteolysis, mass spectroscopy, and physicochemical analysis define this domain as a genuine autonomously folding domain. Our data show that the FHA domain is shorter than previously reported since the C-terminal alpha-helix is not part of its minimum core. Key amino acids postulated to recognize phosphorylated residues are conserved. These data suggest that the kinesin FHA domains are functional domains involved in protein-protein interactions regulated by phosphorylation.",
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Kinesin subfamily UNC104 contains a FHA domain : boundaries and physicochemical characterization. / Westerholm-Parvinen, A; Vernos, I; Serrano, L.

In: FEBS Letters, Vol. 486, No. 3, 15.12.2000, p. 285-90.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Kinesin subfamily UNC104 contains a FHA domain

T2 - boundaries and physicochemical characterization

AU - Westerholm-Parvinen, A

AU - Vernos, I

AU - Serrano, L

PY - 2000/12/15

Y1 - 2000/12/15

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AB - By sequence analysis we show that the U104 domain found in the UNC104 subfamily of kinesins is a forkhead homology-associated domain (FHA). A combination of limited proteolysis, mass spectroscopy, and physicochemical analysis define this domain as a genuine autonomously folding domain. Our data show that the FHA domain is shorter than previously reported since the C-terminal alpha-helix is not part of its minimum core. Key amino acids postulated to recognize phosphorylated residues are conserved. These data suggest that the kinesin FHA domains are functional domains involved in protein-protein interactions regulated by phosphorylation.

KW - Forkhead homology-associated domain

KW - Xenopuskinesin-like protein 4

KW - Kinesin-like protein

KW - UNC104 subfamily

U2 - 10.1016/s0014-5793(00)02310-3

DO - 10.1016/s0014-5793(00)02310-3

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