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

Andŕe Düselder, Vladimir Fridman, Christina Thiede, Alice Wiesbaum, Alina Goldstein, D.R. Klopfenstein, Olga Zaitseva, M.E. Janson, Larisa Gheber*, C.F. Schmidt

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

8 Citations (Scopus)

Abstract

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 languageEnglish
Pages (from-to)16841-16850
JournalJournal of Biological Chemistry
Volume290
Issue number27
DOIs
Publication statusPublished - 3 Jul 2015

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