A Novel Structural Unit in the N-terminal Region of Filamins

Sethi, Ritika; Seppälä, Jonne; Tossavainen, Helena; Ylilauri, Mikko; Ruskamo, Salla; Pentikäinen, Olli T.; Pentikäinen, Ulla; Permi, Perttu; Ylänne, Jari

doi:10.1074/jbc.m113.537456

Cited by 20 publications

(25 citation statements)

References 72 publications

(81 reference statements)

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“…We have recently reported that domain 4 is stabilized by interaction with the neighboring domains [16]. Here, we did not observe interactions with FLNc domain 9 with its neighbors.…”

Section: Discussioncontrasting

confidence: 64%

Small-Angle X-Ray Scattering Reveals Compact Domain-Domain Interactions in the N-Terminal Region of Filamin C

Sethi

Ylänne

2014

PLoS ONE

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Filamins are multi-domain, actin cross-linking, and scaffolding proteins. In addition to the actin cross-linking function, filamins have a role in mechanosensor signaling. The mechanosensor function is mediated by domain-domain interaction in the C-terminal region of filamins. Recently, we have shown that there is a three-domain interaction module in the N-terminal region of filamins, where the neighboring domains stabilize the structure of the middle domain and thereby regulate its interaction with ligands. In this study, we have used small-angle X-ray scattering as a tool to screen for potential domain-domain interactions in the N-terminal region. We found evidence of four domain-domain interactions with varying flexibility. These results confirm our previous study showing that domains 3, 4, and 5 exist as a compact three domain module. In addition, we report interactions between domains 11–12 and 14–15, which are thus new candidate sites for mechanical regulation.

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“…We have recently reported that domain 4 is stabilized by interaction with the neighboring domains [16]. Here, we did not observe interactions with FLNc domain 9 with its neighbors.…”

Section: Discussioncontrasting

confidence: 64%

Small-Angle X-Ray Scattering Reveals Compact Domain-Domain Interactions in the N-Terminal Region of Filamin C

Sethi

Ylänne

2014

PLoS ONE

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“…Because the whole crystal structure of FLN c lacked in the protein data bank, FLN c was modelled by five separate modelled structures: I (template: 2K7P, amino acid positions: 1‐187), II (template: 5DCP, amino acid positions: 158‐236), III (template: 2J3S, amino acid positions: 237‐519), IV (template: 3V8O, amino acid positions: 430‐615), and V (template: 4M9P, amino acid positions: 619‐837) . Three peptides were included in one epitope in region II, which was formed around the key amino acid I 295 /A 296 .…”

Section: Resultsmentioning

confidence: 99%

“…(Figure 7). 32 Three peptides were included in one epitope in region II, which was formed around the key amino acid I 295 /A 296 .…”

Section: Identification and Alignment Of Ige Mimotopes Of Myosinogementioning

confidence: 99%

A comprehensive analysis of the allergenicity and IgE epitopes of myosinogen allergens in Scylla paramamosain

Yang

Jin

et al. 2018

Clin Experimental Allergy

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“…Although the repeats were predicted to be linearly aligned to form rods (rod-1, R1-R15; rod-2, R16-R23, Figure 2) based on the V-shaped structure of the purified FLNA molecule [25], structural analysis of the shorter fragments of the rods revealed domain-domain pairs in R3-R5, R16-R17, R18-R19, and R20-R21 [26][27][28][29] (Figure 2). Small-angle X-ray scattering revealed a compact structure in FLNC R3-R5 and possibly in R11-R12 and R14-R15 [29,30]. These domain pairs can be unfolded by mechanical forces to expose cryptic binding site as discussed below (mechanotransduction).…”

Section: Structure Of Filamin C (Flnc) and Its Family Proteinsmentioning

confidence: 99%

Structure and Function of Filamin C in the Muscle Z-Disc

Mao

Nakamura

2020

IJMS

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Filamin C (FLNC) is one of three filamin proteins (Filamin A (FLNA), Filamin B (FLNB), and FLNC) that cross-link actin filaments and interact with numerous binding partners. FLNC consists of a N-terminal actin-binding domain followed by 24 immunoglobulin-like repeats with two intervening calpain-sensitive hinges separating R15 and R16 (hinge 1) and R23 and R24 (hinge-2). The FLNC subunit is dimerized through R24 and calpain cleaves off the dimerization domain to regulate mobility of the FLNC subunit. FLNC is localized in the Z-disc due to the unique insertion of 82 amino acid residues in repeat 20 and necessary for normal Z-disc formation that connect sarcomeres. Since phosphorylation of FLNC by PKC diminishes the calpain sensitivity, assembly, and disassembly of the Z-disc may be regulated by phosphorylation of FLNC. Mutations of FLNC result in cardiomyopathy and muscle weakness. Although this review will focus on the current understanding of FLNC structure and functions in muscle, we will also discuss other filamins because they share high sequence similarity and are better characterized. We will also discuss a possible role of FLNC as a mechanosensor during muscle contraction.

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A Novel Structural Unit in the N-terminal Region of Filamins

Cited by 20 publications

References 72 publications

Small-Angle X-Ray Scattering Reveals Compact Domain-Domain Interactions in the N-Terminal Region of Filamin C

Small-Angle X-Ray Scattering Reveals Compact Domain-Domain Interactions in the N-Terminal Region of Filamin C

A comprehensive analysis of the allergenicity and IgE epitopes of myosinogen allergens in Scylla paramamosain

Structure and Function of Filamin C in the Muscle Z-Disc

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