In the article, “Loss of actomyosin regulation in distal arthrogryposis myopathy due to mutant myosin binding protein-C slow,” by Maegen A. Ackermann, Puja D. Patel, Jane Valenti, Yasuharu Tagaki, Earl Homsher, James R. Sellers, and Aikaterini Kontrogianni-Konstantopoulos, in FASEB J. August 2013 27:3217–3228 (doi: 10.1096/fj.13-228882), there are errors in the “Input Protein” included in Figs. 4A, D and 5A, B. These errors do not change the results shown in Figs. 4 and 5 or the conclusions drawn from the study.
The corrected images and legends are as follows:
Figure 4.
Alternative splicing within the C7 domain has no effect on actomyosin interactions; however, alternative splicing within the C10 domain affects its ability to interact with thick filaments. A, D) C7 (A) and C10 (D) domain constructs of sMyBP-C (C7aa720–823 and C7Δ763–780aa720–823, A; and C10aa1016–1127 and C10Δ1107–1127aa1016–1127, D) were assessed for their ability to interact with endogenous myosin and actin in GST pulldown assays. E, F) Far-Western blot (E) and slot blot (F) assays were also performed with the C10 domain constructs (C10aa1016–1127 and C10Δ1107–1127aa1016–1127) to assay for direct interactions with actin and HMM. Although the COOH terminus of sMyBP-C is complexed with myosin and actin filaments in a variant-specific manner (D), it is not able to directly interact with HMM or actin (B). B, C, G, H) In vitro motility assays were used to measure the sliding velocity of actin filaments over a surface coated with HMM in the presence or absence of the C7 (C7aa720–823 and C7Δ763–780aa720–823; B, C) and C10 (C10aa1016–1127 and C10Δ1107–1127aa1016–1127; G, H) domain proteins. B, G) Bar graphs indicate the percentage change in the sliding velocity of actin filaments normalized to sham conditions. C, H) Bar graphs depict the percentage ± se of available actin at the gliding surface 75 s following addition of the sMyBP-C proteins. Insets: representative snapshots of the gliding surface 75 s following the addition of the proteins at 1 μM. *P < 0.01 vs. sham treatment; t test.
Figure 5.
COOH terminus of sMyBP-C mediates binding to thick filaments but fails to support binding in the presence of the Y856H DA-1 mutation. A) GST pulldown assays were used to assess the ability of the extended COOH-terminal constructs of sMyBP-C (C8–C10aa854–1127 and C8–C10Δ1107–1127aa854–1127) to interact with endogenous myosin and actin. B) COOH-terminal constructs of sMyBP-C carrying the Y856H DA-1 mutation (C8–C10Y856Haa854–1127 and C8–C10Δ1107–1127 Y856Haa854–1127) were assessed for their ability to interact with endogenous myosin and actin. The presence of the Y856H DA-1 mutation abolishes all binding activity.
These errors have been corrected online. The authors regret any inconvenience caused by these errors.
DOI: 10.1096/fj.13-228882ERR
