TY - JOUR
T1 - Regulation of a heterodimeric kinesin-2 through an unprocessive motor domain that is turned processive by its partner
AU - Brunnbauer, Melanie
AU - Mueller-Planitz, Felix
AU - Kösem, Süleyman
AU - Ho, Thi Hieu
AU - Dombi, Renate
AU - Gebhardt, J. Christof M.
AU - Rief, Matthias
AU - Ökten, Zeynep
PY - 2010/6/8
Y1 - 2010/6/8
N2 - Cilia are microtubule-based protrusions of the plasma membrane found on most eukaryotic cells. Their assembly is mediated through the conserved intraflagellar transport mechanism. One class of motor proteins involved in intraflagellar transport, kinesin-2, is unique among kinesin motors in that some of its members are composed of two distinct polypeptides. However, the biological reason for heterodimerization has remained elusive. Here we provide several interdependent reasons for the heterodimerization of the kinesin-2 motor KLP11/KLP20 of Caenorhabditis elegans cilia. One motor domain is unprocessive as a homodimer, but heterodimerization with a processive partner generates processivity. The "unprocessive" subunit is kept in this partnership as it mediates an asymmetric autoregulation of the motor activity. Finally, heterodimerization is necessary to bind KAP1, the in vivo link between motor and cargo.
AB - Cilia are microtubule-based protrusions of the plasma membrane found on most eukaryotic cells. Their assembly is mediated through the conserved intraflagellar transport mechanism. One class of motor proteins involved in intraflagellar transport, kinesin-2, is unique among kinesin motors in that some of its members are composed of two distinct polypeptides. However, the biological reason for heterodimerization has remained elusive. Here we provide several interdependent reasons for the heterodimerization of the kinesin-2 motor KLP11/KLP20 of Caenorhabditis elegans cilia. One motor domain is unprocessive as a homodimer, but heterodimerization with a processive partner generates processivity. The "unprocessive" subunit is kept in this partnership as it mediates an asymmetric autoregulation of the motor activity. Finally, heterodimerization is necessary to bind KAP1, the in vivo link between motor and cargo.
KW - Molecular motors
KW - Optical tweezers
KW - Single molecule
UR - http://www.scopus.com/inward/record.url?scp=77953762901&partnerID=8YFLogxK
U2 - 10.1073/pnas.1005177107
DO - 10.1073/pnas.1005177107
M3 - Article
AN - SCOPUS:77953762901
SN - 0027-8424
VL - 107
SP - 10460
EP - 10465
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 23
ER -