The C-termini of tubulin and the specific geometry of tubulin substrates influence the depolymerization activity of MCAK

Kathleen M. Hertzer, Claire Walczak

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

MCAK is a Kinesin-13 that depolymerizes microtubules (MTs) and regulates MT dynamics. We used subtilisin-treated MTs (MTs lacking the C-termini of α- and β-tubulin) and alternative tubulin substrates to study which structural and geometrical features of the MT are critical for MCAK activity. We found that removal of the C-termini significantly decreased the efficiency of MCAK-induced depolymerization, which was not due to a reduction of end-specific binding. We also found that depolymerization of SMTs led to an increase in the stabilization of curved oligomeric tubulin products. Using alternative tubulin substrates with different geometries, we found that MCAK depolymerized parallel and anti-parallel tubulin sheets. However, MCAK did not depolymerize tubulin rings regardless of the presence or absence of the tubulin C-termini. We propose that localization of MCAK to the ends of MTs is independent of tubulin C-termini, that MCAK stabilizes a curved conformation at the end of the MT, and that efficient release of this complex is dependent on the presence of the C-termini of tubulin.

Original languageEnglish
Pages (from-to)2727-2737
Number of pages11
JournalCell Cycle
Volume7
Issue number17
StatePublished - Sep 1 2008

Fingerprint

Depolymerization
Tubulin
Microtubules
Geometry
Substrates
Subtilisin
Kinesin
Surface mount technology
Conformations
Stabilization

Keywords

  • Kinesin
  • Microtubules
  • Mitosis
  • Mitotic spindle
  • Motor protein

ASJC Scopus subject areas

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Cite this

The C-termini of tubulin and the specific geometry of tubulin substrates influence the depolymerization activity of MCAK. / Hertzer, Kathleen M.; Walczak, Claire.

In: Cell Cycle, Vol. 7, No. 17, 01.09.2008, p. 2727-2737.

Research output: Contribution to journalArticle

@article{1fb09bc9b09341749b6786cd0d5066ea,
title = "The C-termini of tubulin and the specific geometry of tubulin substrates influence the depolymerization activity of MCAK",
abstract = "MCAK is a Kinesin-13 that depolymerizes microtubules (MTs) and regulates MT dynamics. We used subtilisin-treated MTs (MTs lacking the C-termini of α- and β-tubulin) and alternative tubulin substrates to study which structural and geometrical features of the MT are critical for MCAK activity. We found that removal of the C-termini significantly decreased the efficiency of MCAK-induced depolymerization, which was not due to a reduction of end-specific binding. We also found that depolymerization of SMTs led to an increase in the stabilization of curved oligomeric tubulin products. Using alternative tubulin substrates with different geometries, we found that MCAK depolymerized parallel and anti-parallel tubulin sheets. However, MCAK did not depolymerize tubulin rings regardless of the presence or absence of the tubulin C-termini. We propose that localization of MCAK to the ends of MTs is independent of tubulin C-termini, that MCAK stabilizes a curved conformation at the end of the MT, and that efficient release of this complex is dependent on the presence of the C-termini of tubulin.",
keywords = "Kinesin, Microtubules, Mitosis, Mitotic spindle, Motor protein",
author = "Hertzer, {Kathleen M.} and Claire Walczak",
year = "2008",
month = "9",
day = "1",
language = "English",
volume = "7",
pages = "2727--2737",
journal = "Cell Cycle",
issn = "1538-4101",
publisher = "Landes Bioscience",
number = "17",

}

TY - JOUR

T1 - The C-termini of tubulin and the specific geometry of tubulin substrates influence the depolymerization activity of MCAK

AU - Hertzer, Kathleen M.

AU - Walczak, Claire

PY - 2008/9/1

Y1 - 2008/9/1

N2 - MCAK is a Kinesin-13 that depolymerizes microtubules (MTs) and regulates MT dynamics. We used subtilisin-treated MTs (MTs lacking the C-termini of α- and β-tubulin) and alternative tubulin substrates to study which structural and geometrical features of the MT are critical for MCAK activity. We found that removal of the C-termini significantly decreased the efficiency of MCAK-induced depolymerization, which was not due to a reduction of end-specific binding. We also found that depolymerization of SMTs led to an increase in the stabilization of curved oligomeric tubulin products. Using alternative tubulin substrates with different geometries, we found that MCAK depolymerized parallel and anti-parallel tubulin sheets. However, MCAK did not depolymerize tubulin rings regardless of the presence or absence of the tubulin C-termini. We propose that localization of MCAK to the ends of MTs is independent of tubulin C-termini, that MCAK stabilizes a curved conformation at the end of the MT, and that efficient release of this complex is dependent on the presence of the C-termini of tubulin.

AB - MCAK is a Kinesin-13 that depolymerizes microtubules (MTs) and regulates MT dynamics. We used subtilisin-treated MTs (MTs lacking the C-termini of α- and β-tubulin) and alternative tubulin substrates to study which structural and geometrical features of the MT are critical for MCAK activity. We found that removal of the C-termini significantly decreased the efficiency of MCAK-induced depolymerization, which was not due to a reduction of end-specific binding. We also found that depolymerization of SMTs led to an increase in the stabilization of curved oligomeric tubulin products. Using alternative tubulin substrates with different geometries, we found that MCAK depolymerized parallel and anti-parallel tubulin sheets. However, MCAK did not depolymerize tubulin rings regardless of the presence or absence of the tubulin C-termini. We propose that localization of MCAK to the ends of MTs is independent of tubulin C-termini, that MCAK stabilizes a curved conformation at the end of the MT, and that efficient release of this complex is dependent on the presence of the C-termini of tubulin.

KW - Kinesin

KW - Microtubules

KW - Mitosis

KW - Mitotic spindle

KW - Motor protein

UR - http://www.scopus.com/inward/record.url?scp=50849101069&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=50849101069&partnerID=8YFLogxK

M3 - Article

C2 - 18758237

AN - SCOPUS:50849101069

VL - 7

SP - 2727

EP - 2737

JO - Cell Cycle

JF - Cell Cycle

SN - 1538-4101

IS - 17

ER -