Cordon Bleu serves as a platform at the basal region of microvilli, where it regulates microvillar length through its WH2 domains

Wayt, Jessica; Bretscher, Anthony

doi:10.1091/mbc.e14-06-1131

Cited by 31 publications

(57 citation statements)

References 37 publications

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“…Cobl is enriched in the brain, where it plays an important role in dendritic arborization [9, 24, 25]. Cobl's nucleation activity has also been linked to primary cilia formation [26, 27] and microvillar assembly [28] and length regulation [29]. …”

Section: Opinionmentioning

confidence: 99%

“…However, actin is one of the most abundant proteins in nature whereas Cobl appears to be expressed at low levels (The Human Protein Atlas), suggesting that such high ratios of Cobl to actin are unlikely to occur under physiological conditions. It thus remains to be tested whether Cobl's primary physiological activity is nucleation [9, 24, 28, 29] or filament severing and monomer sequestration [30] (see Outstanding Questions).…”

Section: Opinionmentioning

confidence: 99%

“…Remarkably, the cellular activities of Cobl depend on interactions with several cofactors, which are all expected to form dimers and would thus induce Cobl dimerization. This includes the BAR domain proteins syndapin, SNX9 and ASAP1 [24, 28, 29] as well as Abp1 [25], a protein featuring a predicted coiled coil domain in the middle of the sequence. All these proteins contain SH3 domains, which appear to interact with Cobl's PRDs.…”

Section: Opinionmentioning

confidence: 99%

“…For Spire-Cappuccino [2], VopL/VopF [21, 33, 34] and Sca2 [39] similar mechanisms have been proposed, and are supported by structural and biochemical data. The mechanism proposed for Cobl is only supported by cellular data showing strict cooperation between Cobl and dimeric BAR domain proteins [24, 28, 29], and the widespread importance of dimerization (oligomerization) among filament nucleators. Except in the case of formins and Sca2, which function both as nucleation and elongation factors, these proteins are thought to be dissociate after nucleation, which is at least in part due to competition between binding of the WH2 domain and inter-subunit contacts in the filament (Figure S1).…”

Section: Figurementioning

confidence: 99%

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The WH2 Domain and Actin Nucleation: Necessary but Insufficient

Domínguez

2016

Trends in Biochemical Sciences

117

144

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Two types of sequences, proline-rich domains (PRDs) and the WASP-Homology 2 (WH2) domain, are found in most actin filament nucleation and elongation factors discovered thus far. PRDs serve as a platform for protein-protein interactions, often mediating the binding of profilin-actin. The WH2 domain is an abundant actin monomer-binding motif consisting of ~17-aa. It frequently occurs in tandem repeats, and functions in nucleation by recruiting actin subunits to form the polymerization nucleus. It is found in Spire, Cobl, Lmod, Arp2/3 complex activators (WASP, WHAMM, WAVE, etc.), the bacterial nucleators VopL/VopF and Sca2 and some formins. Yet, it is argued here that the WH2 domain plays only an auxiliary role in nucleation, always synergizing with other domains or proteins for this activity.

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Section: Opinionmentioning

confidence: 99%

Section: Opinionmentioning

confidence: 99%

Section: Opinionmentioning

confidence: 99%

Section: Figurementioning

confidence: 99%

See 2 more Smart Citations

The WH2 Domain and Actin Nucleation: Necessary but Insufficient

Domínguez

2016

Trends in Biochemical Sciences

117

144

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“…A cordon-bleu WH2 repeat protein ( COBL ) gene was found in close proximity to the significant SNPs. COBL is a member of the G/F-actin binding protein family, which act as actin nucleators (Renault et al, 2008; Campellone and Welch, 2010; Wayt and Bretscher, 2014). G- and F-actin are constituents of myofibrils, which are small membraneless parallel fibers in muscle (Murray, 1995).…”

Section: Resultsmentioning

confidence: 99%

Validation of Single Nucleotide Polymorphisms Associated with Carcass Traits in a Commercial Hanwoo Population

Sudrajad

Sharma²,

Dang³

et al. 2016

Asian Australas. J. Anim. Sci

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Four carcass traits, namely carcass weight (CW), eye muscle area (EMA), back fat thickness (BF), and marbling score (MS), are the main price decision parameters used for purchasing Hanwoo beef. The development of DNA markers for these carcass traits for use in a beef management system could result in substantial profit for beef producers in Korea. The objective of this study was to validate the association of highly significant single nucleotide polymorphisms (SNPs) identified in a previous genome-wide association study (GWAS) with the four carcass traits in a commercial Hanwoo population. We genotyped 83 SNPs distributed across all 29 autosomes in 867 steers from a Korean Hanwoo feedlot. Six SNPs, namely ARS-BFGL-NGS-22774 (Chr4, Pos:4889229), ARS-BFGL-NGS-100046 (Chr6, Pos:61917424), ARS-BFGL-NGS-39006 (Chr27, Pos:38059196), ARS-BFGL-NGS-18790 (Chr10, Pos:26489109), ARS-BFGL-NGS-43879 (Chr9, Pos:39964297), and BTB-00775794 (Chr20, Pos:20476265), were found to be associated with CW, EMA, BF, and MS. The ARS-BFGL-NGS-22774, BTB-00775794, and ARS-BFGL-NGS-39006 markers accounted for 1.80%, 1.72%, and 1.35% (p<0.01), respectively, of the phenotypic variance in the commercial Hanwoo population. Many genes located in close proximity to the significant SNPs identified in this study were previously reported to have roles in carcass traits. The results of this study could be useful for marker-assisted selection programs.

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Impact of cordon‐bleu expression on actin cytoskeleton architecture and dynamics

2016

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Cordon-bleu (COBL) is a multifunctional WASP-Homology 2 (WH2) domain-containing protein implicated in a wide variety of cellular functions ranging from dendritic arborization in neurons to the assembly of microvilli on the surface of transporting epithelial cells. In vitro biochemical studies suggest that COBL is capable of nucleating and severing actin filaments, among other activities. How the multiple activities of COBL observed in vitro contribute to its function in cells remains unclear. Here, we used live imaging to evaluate the impact of COBL expression on the actin cytoskeleton in cultured cells. We found that COBL induces the formation of dynamic linear actin structures throughout the cytosol. We also found that stabilizing these dynamic structures with the parallel actin bundling protein espin slows down their turnover and enables the robust formation of self-supported protrusions on the dorsal cell surface. Super-resolution imaging revealed a global remodeling of the actin cytoskeleton in cells expressing these two factors. Taken together, these results provide insight as to how COBL contributes to the assembly of actin-based structures such as epithelial microvilli.

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Cordon Bleu serves as a platform at the basal region of microvilli, where it regulates microvillar length through its WH2 domains

Cited by 31 publications

References 37 publications

The WH2 Domain and Actin Nucleation: Necessary but Insufficient

The WH2 Domain and Actin Nucleation: Necessary but Insufficient

Validation of Single Nucleotide Polymorphisms Associated with Carcass Traits in a Commercial Hanwoo Population

Impact of cordon‐bleu expression on actin cytoskeleton architecture and dynamics

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