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

doi:10.1074/jbc.M114.620799

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 journal › Article › Academic › peer-review

16 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 language	English
Pages (from-to)	16841-16850
Journal	Journal of Biological Chemistry
Volume	290
Issue number	27
DOIs	https://doi.org/10.1074/jbc.M114.620799
Publication status	Published - 3 Jul 2015

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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.",

author = "And{\'r}e D{\"u}selder and Vladimir Fridman and Christina Thiede and Alice Wiesbaum and Alina Goldstein and D.R. Klopfenstein and Olga Zaitseva and M.E. Janson and Larisa Gheber and C.F. Schmidt",

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T1 - Deletion of the tail domain of the kinesin-5 Cin8 affects its directionality

AU - Düselder, Andŕe

AU - Fridman, Vladimir

AU - Thiede, Christina

AU - Wiesbaum, Alice

AU - Goldstein, Alina

AU - Klopfenstein, D.R.

AU - Zaitseva, Olga

AU - Janson, M.E.

AU - Gheber, Larisa

AU - Schmidt, C.F.

PY - 2015/7/3

Y1 - 2015/7/3

N2 - 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.

AB - 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.

U2 - 10.1074/jbc.M114.620799

DO - 10.1074/jbc.M114.620799

M3 - Article

AN - SCOPUS:84936803659

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VL - 290

SP - 16841

EP - 16850

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 27

ER -

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

Abstract

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