The cardiac ankyrin repeat domain 1 protein: do you know enough about its dimerization properties?

Михайлов, А. И.; Torrado, Mario

doi:10.1007/s10974-006-9061-x

Cited by 3 publications

(3 citation statements)

References 4 publications

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“…Later this data was confirmed and extended by other approaches (Witt et al, 2005;Torrado et al, 2008). The ANKRD1-ANKRD1 self-interaction represents a weak interaction (Witt et al, 2005;Mikhailov and Torrado, 2006) thus reducing the probability that in cardiomyocytes ANKRD1/CARP oligomerization via the coiledcoil domain could be sufficient to promote a stable multivalent interaction of ANKRD1/CARP dimers with two or more molecules, permitting those molecules to function in a coordinated way.…”

Section: Introductionmentioning

confidence: 59%

The enigmatic role of the ankyrin repeat domain 1 gene in heart development and disease

Михайлов¹,

Torrado²

2008

Int. J. Dev. Biol.

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It has been proposed that the ankyrin repeat domain 1 (ANKRD1) factor (also known as CARP) plays a critical role in transcriptional regulation, myofibrillar assembly and stretch sensing during heart development and cardiac insults. ANKRD1/CARP has also been reported to negatively regulate cardiac gene expression in cell-based promoter-reporter assays. Consequently, rapid up-regulation of the ankrd1 gene in myocardium in response to developmental stimuli or pathological insults has tended to be interpreted in the context of the inhibitory effects of ANKRD1 on cardiomyocyte gene expression. Surprisingly, a total ankrd1 knockout resulted in a complete lack of phenotype, suggesting that ANKRD1/CARP is not crucial for regulation of cardiac gene expression in vivo. In this essay, we summarize (1) the accumulated evidence for the apparent multifunctional properties of this enigmatic protein, (2) the distinct chamber-dependent regulation of ankrd1 expression patterns in the heart, both during development and cardiac injury, and (3) ANKRD1 involvement in networks regulating adaptation of the myocardium to stress. Whenever feasible, we present the results obtained in patients together with those obtained in the relevant animal and cellular models. A close examination of the findings still fails to define ANKRD1 as a negative regulator of cardiac gene expression in vivo, but rather indicates that its augmented expression can represent an adaptive response of the myocardium to stress both during development and various heart insults.

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Section: Introductionmentioning

confidence: 59%

The enigmatic role of the ankyrin repeat domain 1 gene in heart development and disease

Михайлов¹,

Torrado²

2008

Int. J. Dev. Biol.

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“…ANKRD1 belongs to a conserved family of muscle ankyrin repeat proteins, along with ANKRD2 and ANKRD23 (9). ANKRD1 acts as a transcriptional regulator of the Nkx2.5 pathway during cardiomyogenesis (10), and ANKRD1 expression is regulated by cardiac overload, hypertension, and heart failure in the adult heart (7,10).…”

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confidence: 99%

ANKRD1 Acts as a Transcriptional Repressor of MMP13 via the AP-1 Site

Almodóvar-García

Kwon

Samaras

et al. 2014

Molecular and Cellular Biology

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“…No fluorescence was detected in control cells cotransformed with NGFP-NT-ANKRD1 + CT-ANKRD1-CGFP (data not shown). Given that the ANKRD1 dimerization seems to be a weak interaction (9,10), the results highlight the sensitivity of the modified GFP reassembly assay.…”

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confidence: 82%

Detection of Protein Interactions Based on GFP Fragment Complementation by Fluorescence Microscopy and Spectrofluorometry

2008

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We have developed a set of simple modifications of the green fluorescent protein (GFP) fragment reassembly assay in bacteria that permits: (i) fluorescent microscopy visualization of GFP reassembly only 1-2 h after induction of protein expression, thus approximating the detection of GFP reassembly to the real-time dynamics of protein complex formation in living cells; (ii) spectrofluorometric detection of reassembled GFP fluorescent signals directly in lysates from cell suspension thereby avoiding, in many cases, the need for tag-affinity isolation of protein complexes; and (iii) comparative quantification of signal intensity in numerous cell-sample lysates using a Bio-Rad IQ5 spectrofluorometric detection system (Bio-Rad Laboratories, Madrid, Spain). Collectively, the results demonstrate that the combination of microscopic and spectrofluorometric detection provides a time-saving and sensitive alternative to existing methods of fluorescence complementation analysis.

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The cardiac ankyrin repeat domain 1 protein: do you know enough about its dimerization properties?

Cited by 3 publications

References 4 publications

The enigmatic role of the ankyrin repeat domain 1 gene in heart development and disease

The enigmatic role of the ankyrin repeat domain 1 gene in heart development and disease

ANKRD1 Acts as a Transcriptional Repressor of MMP13 via the AP-1 Site

Detection of Protein Interactions Based on GFP Fragment Complementation by Fluorescence Microscopy and Spectrofluorometry

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