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

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, Dieter R. Klopfenstein, Olga Zaitseva, Marcel E. Janson, Larisa Gheber, Christoph F. Schmidt

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

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
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	290
Issue number	27
DOIs	https://doi.org/10.1074/jbc.M114.620799
State	Published - 3 Jul 2015

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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title = "Deletion of the tail domain of the kinesin-5 Cin8 affects its directionality",

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 Klopfenstein, {Dieter R.} and Olga Zaitseva and Janson, {Marcel E.} and Larisa Gheber and Schmidt, {Christoph F.}",

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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, Dieter R.

AU - Zaitseva, Olga

AU - Janson, Marcel E.

AU - Gheber, Larisa

AU - Schmidt, Christoph 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.

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U2 - 10.1074/jbc.M114.620799

DO - 10.1074/jbc.M114.620799

M3 - Article

AN - SCOPUS:84936803659

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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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