TY - JOUR
T1 - Dynamin 2 and BAR domain protein pacsin 2 cooperatively regulate formation and maturation of podosomes
AU - Li, Jianzhen
AU - Fujise, Kenshiro
AU - Wint, Haymar
AU - Senju, Yosuke
AU - Suetsugu, Shiro
AU - Yamada, Hiroshi
AU - Takei, Kohji
AU - Takeda, Tetsuya
N1 - Funding Information:
This work was supported by JSPS KAKENHI ( 18K07198 and 19KK0180 ), grants from Wesco Scientific Promotion Foundationand Ryobi Teien Memory Foundation for T.T. and JSPS KAKENNHI ( 19H03225 ) for K.T.
Publisher Copyright:
© 2021 Elsevier Inc.
PY - 2021/9/24
Y1 - 2021/9/24
N2 - Podosomes are actin-rich adhesion structures formed in a variety of cell types, such as monocytic cells or cancer cells, to facilitate attachment to and degradation of the extracellular matrix (ECM). Previous studies showed that dynamin 2, a large GTPase involved in membrane remodeling and actin organization, is required for podosome function. However, precise roles of dynamin 2 at the podosomes remain to be elucidated. In this study, we identified a BAR (Bin-Amphiphysin-Rvs167) domain protein pacsin 2 as a functional partner of dynamin 2 at podosomes. Dynamin 2 and pacsin 2 interact and co-localize to podosomes in Src-transformed NIH 3T3 (NIH-Src) cells. RNAi of either dynamin 2 or pacsin 2 in NIH-Src cells inhibited podosome formation and maturation, suggesting essential and related roles at podosomes. Consistently, RNAi of pacsin 2 prevented dynamin 2 localization to podosomes, and reciprocal RNAi of dynamin 2 prevented pacsin 2 localization to podosomes. Taking these results together, we conclude that dynamin 2 and pacsin 2 co-operatively regulate organization of podosomes in NIH-Src cells.
AB - Podosomes are actin-rich adhesion structures formed in a variety of cell types, such as monocytic cells or cancer cells, to facilitate attachment to and degradation of the extracellular matrix (ECM). Previous studies showed that dynamin 2, a large GTPase involved in membrane remodeling and actin organization, is required for podosome function. However, precise roles of dynamin 2 at the podosomes remain to be elucidated. In this study, we identified a BAR (Bin-Amphiphysin-Rvs167) domain protein pacsin 2 as a functional partner of dynamin 2 at podosomes. Dynamin 2 and pacsin 2 interact and co-localize to podosomes in Src-transformed NIH 3T3 (NIH-Src) cells. RNAi of either dynamin 2 or pacsin 2 in NIH-Src cells inhibited podosome formation and maturation, suggesting essential and related roles at podosomes. Consistently, RNAi of pacsin 2 prevented dynamin 2 localization to podosomes, and reciprocal RNAi of dynamin 2 prevented pacsin 2 localization to podosomes. Taking these results together, we conclude that dynamin 2 and pacsin 2 co-operatively regulate organization of podosomes in NIH-Src cells.
KW - Actin
KW - Dynamin 2
KW - ECM degradation
KW - Pacsin 2
KW - Podosome
UR - http://www.scopus.com/inward/record.url?scp=85111240432&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85111240432&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2021.07.041
DO - 10.1016/j.bbrc.2021.07.041
M3 - Article
C2 - 34325130
AN - SCOPUS:85111240432
SN - 0006-291X
VL - 571
SP - 145
EP - 151
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
ER -
