The filamins

Nakamura, Fumihiko; Stossel, Thomas P.; Hartwig, John H.

doi:10.4161/cam.5.2.14401

Cited by 402 publications

(258 citation statements)

References 123 publications

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“…These results demonstrate that the removal of the 109 AA from the carboxy-terminal end in degraded filamin could be the first cleavage of intact filamin observed in postmortem muscle. The carboxy-terminal end of filamin is responsible for dimerization and interaction with other cellular components such as β integrins, androgen receptors, and portions of potassium channels (Stossel et al, 2001;Feng and Walsh, 2004;Pudas et al, 2005;Nakamura et al, 2011). Therefore, the loss of this carboxy-terminal end causes the loss of ability for this protein to form dimers and impairs anchoring to the Z-line and could impair the structural integrity of the internal architecture of the muscle cell.…”

Section: Discussionmentioning

confidence: 99%

Postmortem protein degradation is a key contributor to fresh pork loin tenderness

Carlson¹,

Prusa²,

Fedler³

et al. 2017

Journal of Animal Science

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The objective of this study was to determine factors that influence tenderness independent of variation in pH, color, or marbling. To achieve the objective, 2 sample groups were chosen from a population of 159 pork loins aged 11 to 16 d. Predetermined ranges (ultimate pH, 5.54 to 5.86; marbling score, 1.0 to 3.0; percent total lipid, 1.61 to 3.37%) were defined for inclusion of individual loins in the study. The pork loins with the greatest (n = 12) and least (n = 12) Instron star probe values were assigned to 2 classification groups. The high star probe group had an average star probe that was 2.8 kg greater than the low star probe group (7.75 vs. 4.95 kg). Pork quality and sensory characteristics of pH, subjective and instrumental color values, cook loss, sensory tenderness, chewiness, juiciness, pork flavor, and off flavor were determined on fresh, never frozen pork chops. Lipid content, sarcomere length, myosin heavy-chain profile, and calpain autolysis were determined. Degradation of troponin-T, desmin, filamin, and titin were evaluated on the protein extracts from each sample. Pork loin pH, subjective color scores, Minolta L values, sarcomere length, and myosin heavychain composition were not different across groups. Chops from the low star probe group had a significantly greater marbling score (2.3 vs. 1.9) and lipid content (2.61 vs. 2.23%). Calpain-1 was completely autolyzed in both high and low star probe samples, demonstrating that calpain-1 potentially had been active in all samples. Low star probe whole-muscle protein extracts had more troponin-T (P < 0.01), desmin (P < 0.01), and filamin degradation (P < 0.01) than high star probe samples. Both classification groups showed degradation of titin. Remarkably, some high star probe samples still had observable intact bands of titin on SDS-PAGE gels. These results demonstrate that significant variation in instrumental tenderness is observed within a moderate pH range. Lipid content and proteolysis both appear to contribute to this variation.

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Section: Discussionmentioning

confidence: 99%

Postmortem protein degradation is a key contributor to fresh pork loin tenderness

Carlson¹,

Prusa²,

Fedler³

et al. 2017

Journal of Animal Science

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“…FLNA is a scaffolding protein with actin cross-linking capacity that couples extracellular signaling to the cellular cytoskeleton (Nakamura et al, 2011). As a result, FLNA regulates diverse aspects of cell development, including filopodia formation in non-neuronal cells (Ohta et al, 1999), growth cone progression in drosophila (Zheng et al, 2011), proliferation of cortical neural progenitors (Carabalona et al, 2012; Lian et al, 2012), and migration of diverse cell types (Baldassarre et al, 2009; Cunningham et al, 1992; Fox et al, 1998; Xu et al, 2010) including developing cortical neurons (Nagano et al, 2004; Sarkisian et al, 2006, 2008).…”

Section: Introductionmentioning

confidence: 99%

MEK-ERK1/2-Dependent FLNA Overexpression Promotes Abnormal Dendritic Patterning in Tuberous Sclerosis Independent of mTOR

Zhang

Bartley

Gong

et al. 2014

Neuron

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Summary Abnormal dendritic complexity is a shared feature of many neurodevelopmental disorders associated with neurological defects. Here, we found that the actin-crosslinking protein filamin A (FLNA) is overexpressed in tuberous sclerosis complex (TSC) mice, a PI3K-mTOR model of neurodevelopmental disease that is associated with abnormal dendritic complexity. Both under-and overexpression of FLNA in wild-type neurons led to more complex dendritic arbors in vivo, suggesting that an optimal level of FLNA expression is required for normal dendritogenesis. In Tsc1null neurons, knocking down FLNA in vivo prevented dendritic abnormalities. Surprisingly, FLNA overexpression in Tsc1null neurons was dependent on MEK1/2 but not mTOR activity despite both pathways being hyperactive. In addition, increasing MEK-ERK1/2 activity led to dendritic abnormalities via FLNA and decreasing MEK-ERK1/2 signaling in Tsc1null neurons rescued dendritic defects. These data demonstrate that altered FLNA expression increases dendritic complexity and contributes to pathologic dendritic patterning in TSC in an mTOR-independent, ERK1/2-dependent manner.

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“…They also act as scaffolds for many transmembrane, signaling, and cytoskeletal proteins [2]. There are three FLN genes in vertebrates.…”

Section: Introductionmentioning

confidence: 99%

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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The filamins

Cited by 402 publications

References 123 publications

Postmortem protein degradation is a key contributor to fresh pork loin tenderness

Postmortem protein degradation is a key contributor to fresh pork loin tenderness

MEK-ERK1/2-Dependent FLNA Overexpression Promotes Abnormal Dendritic Patterning in Tuberous Sclerosis Independent of mTOR

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

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