Deletion of the tail domain of the kinesin-5 Cin8 affects its directionality

Andŕe Düselder, Vladimir Fridman, Christina Thiede, Alice Wiesbaum, Alina Goldstein, Dieter R. Klopfenstein, Olga Zaitseva, Marcel E. Janson, Larisa Gheber, Christoph F. Schmidt

Research output: Contribution to journalArticlepeer-review


Background: Single molecules of the kinesin-5 Cin8 were previously demonstrated to be minus-end-directed under highionic- strength conditions. Results: Under high-ionic-strength conditions, Cin8 lacking the tail domain is bidirectional. Conclusion: The tail domain is one of the factors that regulate Cin8 directionality. Significance: An important structural element was identified that regulates the directionality of kinesin-5 motors.

Original languageAmerican English
Pages (from-to)16841-16850
Number of pages10
JournalJournal of Biological Chemistry
Issue number27
StatePublished - 3 Jul 2015

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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