TY - JOUR
T1 - Two LIM domain proteins and UNC-96 link UNC-97/PINCH to myosin thick filaments in Caenorhabditis elegans muscle
AU - Qadota, Hiroshi
AU - Mercer, Kristina B.
AU - Miller, Rachel K.
AU - Kaibuchi, Kozo
AU - Benian, Guy M.
PY - 2007/11
Y1 - 2007/11
N2 - By yeast two-hybrid screening, we found three novel interactors (UNC-95, LIM-8, and LIM-9) for UNC-97/PINCH in Caenorhabditis elegans. All three proteins contain LIM domains that are required for binding. Among the three interactors, LIM-8 and LIM-9 also bind to UNC-96, a component of sarcomeric M-lines. UNC-96 and LIM-8 also bind to the C-terminal portion of a myosin heavy chain (MHC), MHC A, which resides in the middle of thick filaments in the proximity of M-lines. All interactions identified by yeast two-hybrid assays were confirmed by in vitro binding assays using purified proteins. All three novel UNC-97 interactors are expressed in body wall muscle and by antibodies localize to M-lines. Either a decreased or an increased dosage of UNC-96 results in disorganization of thick filaments. Our previous studies showed that UNC-98, a C2H2 Zn finger protein, acts as a linkage between UNC-97, an integrin-associated protein, and MHC A in myosin thick filaments. In this study, we demonstrate another mechanism by which this linkage occurs: from UNC-97 through LIM-8 or LIM-9/UNC-96 to myosin.
AB - By yeast two-hybrid screening, we found three novel interactors (UNC-95, LIM-8, and LIM-9) for UNC-97/PINCH in Caenorhabditis elegans. All three proteins contain LIM domains that are required for binding. Among the three interactors, LIM-8 and LIM-9 also bind to UNC-96, a component of sarcomeric M-lines. UNC-96 and LIM-8 also bind to the C-terminal portion of a myosin heavy chain (MHC), MHC A, which resides in the middle of thick filaments in the proximity of M-lines. All interactions identified by yeast two-hybrid assays were confirmed by in vitro binding assays using purified proteins. All three novel UNC-97 interactors are expressed in body wall muscle and by antibodies localize to M-lines. Either a decreased or an increased dosage of UNC-96 results in disorganization of thick filaments. Our previous studies showed that UNC-98, a C2H2 Zn finger protein, acts as a linkage between UNC-97, an integrin-associated protein, and MHC A in myosin thick filaments. In this study, we demonstrate another mechanism by which this linkage occurs: from UNC-97 through LIM-8 or LIM-9/UNC-96 to myosin.
UR - https://www.scopus.com/pages/publications/35848949782
UR - https://www.scopus.com/inward/citedby.url?scp=35848949782&partnerID=8YFLogxK
U2 - 10.1091/mbc.E07-03-0278
DO - 10.1091/mbc.E07-03-0278
M3 - Article
C2 - 17761533
AN - SCOPUS:35848949782
SN - 1059-1524
VL - 18
SP - 4317
EP - 4326
JO - Molecular Biology of the Cell
JF - Molecular Biology of the Cell
IS - 11
ER -