TY - JOUR
T1 - Microtubule Minus-End Binding Protein CAMSAP2 and Kinesin-14 Motor KIFC3 Control Dendritic Microtubule Organization
AU - Cao, Yujie
AU - Lipka, Joanna
AU - Stucchi, Riccardo
AU - Burute, Mithila
AU - Pan, Xingxiu
AU - Portegies, Sybren
AU - Tas, Roderick
AU - Willems, Jelmer
AU - Will, Lena
AU - MacGillavry, Harold
AU - Altelaar, Maarten
AU - Kapitein, Lukas C.
AU - Harterink, Martin
AU - Hoogenraad, Casper C.
PY - 2020/3/9
Y1 - 2020/3/9
N2 - Neuronal dendrites are characterized by an anti-parallel microtubule organization. The mechanism that regulates dendritic microtubule organization is still unclear. Cao et al. demonstrate that the microtubule minus-end binding protein CAMSAP2 and kinesin-14 motor KIFC3 work together to organize dendritic microtubules and control dendrite branching. Neuronal dendrites are characterized by an anti-parallel microtubule organization. The mixed oriented microtubules promote dendrite development and facilitate polarized cargo trafficking; however, the mechanism that regulates dendritic microtubule organization is still unclear. Here, we found that the kinesin-14 motor KIFC3 is important for organizing dendritic microtubules and to control dendrite development. The kinesin-14 motor proteins (Drosophila melanogaster Ncd, Saccharomyces cerevisiae Kar3, Saccharomyces pombe Pkl1, and Xenopus laevis XCTK2) are characterized by a C-terminal motor domain and are well described to organize the spindle microtubule during mitosis using an additional microtubule binding site in the N terminus [1–4]. In mammals, there are three kinesin-14 members, KIFC1, KIFC2, and KIFC3. It was recently shown that KIFC1 is important for organizing axonal microtubules in neurons, a process that depends on the two microtubule-interacting domains [5]. Unlike KIFC1, KIFC2 and KIFC3 lack the N-terminal microtubule binding domain and only have one microtubule-interacting domain, the motor domain [6, 7]. Thus, in order to regulate microtubule-microtubule crosslinking or sliding, KIFC2 and KIFC3 need to interact with additional microtubule binding proteins to connect two microtubules. We found that KIFC3 has a dendrite-specific distribution and interacts with microtubule minus-end binding protein CAMSAP2. Depletion of KIFC3 or CAMSAP2 results in increased microtubule dynamics during dendritic development. We propose a model in which CAMSAP2 anchors KIFC3 at microtubule minus ends and immobilizes microtubule arrays in dendrites.
AB - Neuronal dendrites are characterized by an anti-parallel microtubule organization. The mechanism that regulates dendritic microtubule organization is still unclear. Cao et al. demonstrate that the microtubule minus-end binding protein CAMSAP2 and kinesin-14 motor KIFC3 work together to organize dendritic microtubules and control dendrite branching. Neuronal dendrites are characterized by an anti-parallel microtubule organization. The mixed oriented microtubules promote dendrite development and facilitate polarized cargo trafficking; however, the mechanism that regulates dendritic microtubule organization is still unclear. Here, we found that the kinesin-14 motor KIFC3 is important for organizing dendritic microtubules and to control dendrite development. The kinesin-14 motor proteins (Drosophila melanogaster Ncd, Saccharomyces cerevisiae Kar3, Saccharomyces pombe Pkl1, and Xenopus laevis XCTK2) are characterized by a C-terminal motor domain and are well described to organize the spindle microtubule during mitosis using an additional microtubule binding site in the N terminus [1–4]. In mammals, there are three kinesin-14 members, KIFC1, KIFC2, and KIFC3. It was recently shown that KIFC1 is important for organizing axonal microtubules in neurons, a process that depends on the two microtubule-interacting domains [5]. Unlike KIFC1, KIFC2 and KIFC3 lack the N-terminal microtubule binding domain and only have one microtubule-interacting domain, the motor domain [6, 7]. Thus, in order to regulate microtubule-microtubule crosslinking or sliding, KIFC2 and KIFC3 need to interact with additional microtubule binding proteins to connect two microtubules. We found that KIFC3 has a dendrite-specific distribution and interacts with microtubule minus-end binding protein CAMSAP2. Depletion of KIFC3 or CAMSAP2 results in increased microtubule dynamics during dendritic development. We propose a model in which CAMSAP2 anchors KIFC3 at microtubule minus ends and immobilizes microtubule arrays in dendrites.
UR - http://www.scopus.com/inward/record.url?scp=85080941132&partnerID=8YFLogxK
U2 - 10.1016/j.cub.2019.12.056
DO - 10.1016/j.cub.2019.12.056
M3 - Article
SN - 0960-9822
VL - 30
SP - 899-908.e6
JO - Current Biology
JF - Current Biology
IS - 5
ER -