hhLIM is a novel F‐actin binding protein involved in actin cytoskeleton remodeling
Authors: Bin Zheng
Jin-Kun Wen
Mei Han
Journal: FEBS Journal (2008)
Discipline: BIOLOGY & BIOCHEMISTRY
Keywords: hhLIM; actin-binding protein; actin filaments; cytoskeleton; C2C12 cells
Affiliations: Department of Biochemistry and Molecular Biology, Hebei Medical University, Shijiazhuang, China.

Abstract:  Human heart LIM protein (hhLIM) is a newly cloned protein. In vitro analyses showed that green fluorescent protein (GFP)-tagged hhLIM protein accumulated in the cytoplasm of C2C12 cells and colocalized with F-actin, indicating that hhLIM is an actin-binding protein in C2C12 cells. Overexpression of hhLIM-GFP in C2C12 cells significantly stabilized actin filaments and delayed depolymerization of the actin cytoskeleton induced by cytochalasin B treatment. Expression of hhLIM-GFP in C2C12 cells also induced significant changes in the organization of the actin cytoskeleton, specifically, fewer and thicker actin bundles than in control cells, suggesting that hhLIM functions as an actin-bundling protein. This hypothesis was confirmed using low-speed co-sedimentation assays and direct observation of F-actin bundles that formed in vitro in the presence of hhLIM. hhLIM has two LIM domains. To identify the essential regions and sites for association, a series of truncated mutants was constructed which showed that LIM domain 2 has the same activity as full-length hhLIM. To further characterize the binding sites, the LIM domain was functionally destructed by replacing cysteine with serine in domain 2, and results showed that the second LIM domain plays a central role in bundling of F-actin. Taken together, these data identify hhLIM as an actin-binding protein that increases actin cytoskeleton stability by promoting bundling of actin filaments. 

Retracted: No

PubPeer comments:
 We regret to inform you that the following information has been published on pubpeer for peer discussion, prompting the Editor in chief to reconsider his decision. FEBS Ju201d ( hhLIM is a novel F-actin binding protein involved in actin cytoskeleton remodeling. FEBS J. 2008 ;275(7):1568-78. doi: 10.1111 j.1742-4658.2008.06315.x. Figure 4A is the confirmed duplication. The pictures F1, F3, F5, and GST western blot in Fig.4A are similar to F7, F5, and F9 (flipped in parallel) in Fig.4A and Fig. 4B of her other paperuff08Human heart LIM protein activates atrial-natriuretic-factor gene expression by interacting with the cardiac-restricted transcription factor Nkx2.5. Biochem J, 2008, 409: 683-690uff09, and GST s Western blot is the same image. However, the interacted proteins shown in Fig. 4A of the two papers are different, one is Actin, and another one is Nkx2.5. Fig. 4A (FEBS J, 2008; 275: 1568-1578): ![file] Fig.4 uff08Biochem J, 2008, 409: 683-690uff09 ![file] Figure 2D partially duplicated in a subsequent manuscript published in Life Sciences: Smooth muscle 22 alpha maintains the differentiated phenotype of vascular smooth muscle cells by inducing filamentous actin bundling, Life Sci, 2009,84:394-401. The first author stated that Figure 2D (c) is used as a positive control. However, in any part of the paper, there is no explanation of the source and significance of this data. Most notably, SM22u03b1 inducing filamentous actin bundling as an original discovery is published in Life Sci 2009 late than that in 2008 FEBS J paper. Obviously, before being published in 2009suff0cthe data is used as positive control by FEBS J 2008 manuscript. This is not in line with academic convention and is very unreasonable. More seriously, the signature of the corresponding author is not authorized by herself, and the funds marked in the paper are provided by the first and second authors respectively, but not by the corresponding author. The first author has admitted that she generated the illustrations of Figure 4A and Figure 2Duff0cand however not provided any convincing evidence of informed consent of the corresponding author so far. Based on the above mistakes, it is the 2008 FEBS J manuscript that should be retracted instead of the 2009 Life Sci manuscript. Curiously, the Editor in chief of FEBS J rejects the corresponding author rightful request and determines whether a correction or retraction of Figure 2D of the Life Sciences manuscript may be required by the author, correcting Figure 4A, as well as removing Mei Han from the author list. The decision was irresponsible, and damaged the author s due rights and interests. Who will be the actual corresponding author of the Corrigendum text? Let s wait and see. , 
 FEBS J by email (2021-06-24 01:24:43) emphasized that u201cWe do not require all authors to agree to correction of the figure in a Corrigendumu201d, and stated that u201cIf you confirm that you do not want to be removed as an author of the FEBS J paper, we will communicate this to Bin Zheng and Jin Kun Wen and explain that we are waiting for formal resolution of the investigation, communicated via correspondence from the academic committee of Hebei Medical University, before taking further actionu201d. Therefore, we speculated that Bin Zheng and Jin Kun Wen eager to correct Figure 4A, and ask to remove Mei Han from the author list as they were afraid that Mei Han would not agree with the Corrigendum. However, Bin Zheng and Jin Kun Wen assured the academic committee that they had informed Mei Han of the signing of the corresponding author. If this is true, do they have the right to ask for removing Mei Han from the author list. Their internal and external explanations are contradictory, which one is true? Who is the real corresponding author? Bin Zheng or Jin Kun Wen? Why did they sign Mei Han as the corresponding author? Let s wait and see. ,