Erratum to: The extracellular Leucine-Rich Repeat superfamily; a comparative survey and analysis of evolutionary relationships and expression patterns

Dolan, Jackie; Walshe, Karen; Alsbury, Samantha; Hokamp, Karsten; O’Keeffe, Sean; Okafuji, Tatsuya; Miller, Suzanne F.C.; Tear, Guy; Mitchell, Kevin J.

doi:10.1186/1471-2164-10-230

Cited by 3 publications

(2 citation statements)

References 1 publication

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“…LRRC proteins constitute a large protein family. LRRC26 belongs to an extracellular leucine-rich-repeat-only (Elron) cluster (Dolan et al, 2007) that consists of members a single TM segment, an extracellular LRR motif, and a short cytosolic COOH tail containing a stretch of acidic residues (Figure 1B). LRRC proteins have recently begun to gain appreciation as β subunits of K V channels.…”

Section: Bk Channel β Subunitsmentioning

confidence: 99%

Regulation of Voltage-Activated K+ Channel Gating by Transmembrane β Subunits

Sun¹,

Zaydman²,

Cui³

2012

Front. Pharmacol.

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Voltage-activated K+ (KV) channels are important for shaping action potentials and maintaining resting membrane potential in excitable cells. KV channels contain a central pore-gate domain (PGD) surrounded by four voltage-sensing domains (VSDs). The VSDs will change conformation in response to alterations of the membrane potential thereby inducing the opening of the PGD. Many KV channels are heteromeric protein complexes containing auxiliary β subunits. These β subunits modulate channel expression and activity to increase functional diversity and render tissue specific phenotypes. This review focuses on the KV β subunits that contain transmembrane (TM) segments including the KCNE family and the β subunits of large conductance, Ca2+- and voltage-activated K+ (BK) channels. These TM β subunits affect the voltage-dependent activation of KV α subunits. Experimental and computational studies have described the structural location of these β subunits in the channel complexes and the biophysical effects on VSD activation, PGD opening, and VSD–PGD coupling. These results reveal some common characteristics and mechanistic insights into KV channel modulation by TM β subunits.

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Section: Bk Channel β Subunitsmentioning

confidence: 99%

Regulation of Voltage-Activated K+ Channel Gating by Transmembrane β Subunits

Sun¹,

Zaydman²,

Cui³

2012

Front. Pharmacol.

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“…The “LxxLxLxxNxL” motifs located in the inner concave surfaces of the horseshoe-like structure form parallel β-strands, whereas the variable region forms a convex surface generated by α helices, β-turns, and loop structures (Figure 1A). LRR proteins are present in a very large and diverse group of proteins and have been found to be involved in a wide variety of physiological functions including immune responses, signal transduction, cell cycle regulation, enzyme regulation, and transcriptional regulation (Buchanan and Gay, 1996; Dolan et al, 2007). …”

Section: General Structure Of Tlr Ecdsmentioning

confidence: 99%

Similar Structures but Different Roles – An Updated Perspective on TLR Structures

2011

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Toll-like receptors (TLRs) are pattern recognition receptors that recognize conserved structures in pathogens, trigger innate immune responses, and prime antigen-specific adaptive immunity. Elucidation of crystal structures of TLRs interacting with their ligands such as TLR1-2 with triacylated lipopeptide, TLR2-6 with diacylated lipopeptide, TLR4–MD-2 with LPS, and TLR3 with double-stranded RNA (dsRNA) have enabled an understanding of the initiation of TLR signaling. Agonistic ligands such as LPS, dsRNA, and lipopeptides induce “m” shaped TLR dimers in which C-termini converge at the center. Such central convergence is necessary to bring the two intracellular receptor TIR domains closer together and promote their dimerization, which serves as an essential step in downstream signaling. In this review, we summarize TLR ECD structures that have been reported to date with special emphasis on ligand recognition and activation mechanism.

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Membrane proteome characterization of periodontal ligament cell sets from deciduous and permanent teeth

Giovani

Salmon

Martins

et al. 2018

Journal of Periodontology

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Background: Physiological roles for the periodontal ligament (PDL) include tooth eruption and anchorage, force absorption, and provision of proprioceptive information. Despite the advances in understanding the biology of PDL cells, there is a lack of information regarding the molecular signature of deciduous (DecPDL) and permanent (PermPDL) PDL tissues. Thus, the present study was designed to characterize the membrane proteome of DecPDL and PermPDL cells.Methods: Primary PDL cells were obtained (n = 6) and a label-free quantitative proteome of cell membrane-enriched components was performed. Proteome findings were validated by quantitative polymerase chain reaction and Western blot assays in fresh human tissues (n = 8) and primary cell cultures (n = 6). In addition, confocal microscopy was used to verify the expression of target factors in the PDL cell cultures. Results:Comparative gene ontology enrichment analysis evidenced that most stickling differences involved "endomembrane system" (PICALM, STX4, and LRP10), "hydrolase activity" (NCSTN and XRCC6), "protein binding" (PICALM, STX4, GPNMB, VASP, extended-synaptotagmin 2 [ESYT2], and leucine-rich repeat containing 15 [LRRC15]), and "isomerase activity" (FKBP8). Data are available via Pro-teomeXchange with identifier PXD010226. At the transcript level, high PICALM in DecPDL and ESYT2 and LRRC15 in PermPDL were confirmed in fresh PDL tissues. Furthermore, Western blot analysis confirmed increased levels of PICALM, LRRC15, and ESYT2 in cells and/or fresh tissues, and confocal microscopy confirmed the trends for PICALM and LRRC15 expression in PDL cells. Conclusion:We report the first comprehensive characterization of the membrane protein machinery of DecPDL and PermPDL cells, and together, we identified a distinct molecular signature for these cell populations, including unique proteins for DecPDL and PermPDL. K E Y W O R D Scell membrane, deciduous tooth, gene expression, periodontal ligament, permanent dentition, proteomics J Periodontol. 2019;90:775-787.

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Erratum to: The extracellular Leucine-Rich Repeat superfamily; a comparative survey and analysis of evolutionary relationships and expression patterns

Abstract: Correction to Dolan J, Walshe K, Alsbury S, Hokamp K, O'Keeffe S, Okafuji T, Miller SF, Tear G, Mitchell KJ: The extracellular leucine-rich repeat superfamily; a comparative survey and analysis of evolutionary relationships and expression patterns. BMC Genomics 2007, 8:320.

Cited by 3 publications

References 1 publication

Regulation of Voltage-Activated K+ Channel Gating by Transmembrane β Subunits

Regulation of Voltage-Activated K+ Channel Gating by Transmembrane β Subunits

Similar Structures but Different Roles – An Updated Perspective on TLR Structures

Membrane proteome characterization of periodontal ligament cell sets from deciduous and permanent teeth

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