AKAP6
- Known as:
- AKAP6
- Catalog number:
- Y213338
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- AKAP6
Related genes to: AKAP6
- Gene:
- AKAP6 NIH gene
- Name:
- A-kinase anchoring protein 6
- Previous symbol:
- -
- Synonyms:
- KIAA0311, mAKAP, AKAP100, PRKA6, ADAP6
- Chromosome:
- 14q12
- Locus Type:
- gene with protein product
- Date approved:
- 1999-09-16
- Date modifiied:
- 2015-11-17
Related products to: AKAP6
Related articles to: AKAP6
- Heart failure is a major cause of morbidity and mortality worldwide, representing the end stage of cardiovascular diseases that induce pathological cardiac remodeling. At the cellular level, pathological remodeling includes myocyte hypertrophy and decreased survival, changes in myocyte metabolism and contractility, and interstitial myocardial fibrosis, all of which are controlled by a complex network of intracellular signaling pathways. At the outer nuclear envelope of the cardiomyocyte, A-kinase anchoring protein (AKAP) 6β (also known as mAKAPβ) organizes multimolecular signaling complexes called "signalosomes," which include over 25 different signaling enzymes and effector proteins that, in response to cAMP, calcium, and phosphoinositide second messengers, regulate gene expression. The AKAP6β scaffold also binds other scaffold proteins such as AKAP9, permitting higher-order interactions between signaling molecules at the nuclear envelope and adjacent Golgi apparatus. Together, these protein complexes present novel opportunities for compartmentalized inhibition of pathophysiological cardiac remodeling. Both basic molecular mechanisms and potential therapeutic approaches are considered, because this review highlights recent advances in the role of AKAP6 in coordinating compartmentalized signaling and the regulation of cardiomyocyte gene expression promoting heart failure. SIGNIFICANCE STATEMENT: Heart failure is a syndrome of major public health significance. Novel therapies for the treatment of cardiac disease are needed to improve patient quality of life, reduce symptoms, and manage comorbidities associated with heart disease. The A-kinase anchoring protein 6β signalosome has been shown to orchestrate multiple pathological signaling pathways in the cardiomyocyte that induce cardiac disease. Targeting this signalosome should comprise more specific therapeutics for heart failure with fewer side effects than those associated with current treatments. - Source: PubMed
Publication date: 2026/07/24
Aydin SinanKapiloff Michael SDodge-Kafka Kimberly L - To date, effective preventive and therapeutic strategies for early-stage bradyarrhythmia remain limited. - Source: PubMed
Publication date: 2026/07/16
Song Zheng-QiHuang Lu-JieLiu KeWu Sheng-KeChen Jia-RuiPei Yan-ZhenChen Yi-He - During myogenic differentiation, the Microtubule-Organizing Center (MTOC) is relocated to the nuclear envelope by a molecular platform including Linker of Nucleoskeleton and Cytoskeleton (LINC) complex proteins, A Kinase Anchoring Proteins (AKAP9 and AKAP6) and Pericentriolar Material 1 (PCM-1). Here, we show that emerin is required for centrosomal protein recruitment to the nuclear periphery of myonuclei and microtubule dynamics. In fact, in type 1 Emery-Dreifuss Muscular Dystrophy (EDMD1), loss of emerin was associated with altered pericentrin recruitment to the nuclear envelope, LINC protein impairment at the nuclear poles of myonuclei and microtubule organization defects. As a consequence, dynein, mitochondrial distribution and nuclear alignment along the longitudinal axis of the myotubes were altered in EDMD1 myotubes. Moreover, reduced levels of AKAP6 and PKA were detected at the nuclear periphery of EDMD1 myotubes, possibly contributing to an aberrant nuclear localization of the mechanosensing factor YAP. Upon rescue of emerin expression by CRISPR correction of mutated EMD gene: SUN1/2, pericentrin, AKAP6 and PKA were restored at the nuclear envelope and a correct YAP localization was observed in EDMD1 muscle cells. These results show that emerin is required for Nuclear Envelope-MTOC (NE-MTOC) organization in differentiating skeletal muscle cells and suggest that disruption of such complex is a key pathogenetic event in Emery-Dreifuss Muscular Dystrophy. - Source: PubMed
Publication date: 2026/05/12
Mattioli ElisabettaCenni VittoriaSabatelli PatriziaSchena ElisaSanti SpartacoFiorillo ChiaraBruno ClaudioPini AntonellaGiannotta MelaniaCavallo MarcoErrani CostantinoCattin EleonoraBenati DanielaRecchia AlessandraLattanzi Giovanna - Food allergy (FA) arises from a complex interplay between an individual's genetic predisposition and environmental factors, and its prevalence is increasing. Genome-wide association studies to date have been hindered by small sample sizes and varying FA definitions. - Source: PubMed
Publication date: 2026/02/20
Maier LisaSun YidanKronberg JaanikaAbner Erik Coley KayeshaMarenholz IngoWeiss StefanForaita RonjaKarramass TarikMykkänen JuhaHernandez-Pacheco NataliaWang Carol AKitaba Negusse TPechlivanis SonaliBouzigon EmmanuelleTingskov Pedersen Casper-EmilSchoos Ann-Marie MCurtin John AKress SaraHernangomez-Laderas AlbaFoppiano FrancescoAshley SarahBatini ChiaraBryant LukeHomuth GeorgGieger ChristianGilles StefanieLyytikäinen Leo-PekkaRovio SuviPahkala KatjaVernet RaphaëlValenta RudolfLlop SabrinaTorrent MatiesBöck AndreasTang Mimi L KSchmidt-Weber Carsten BMetspalu AndresEsko TõnuSprikkelman Aline BJohn CatherineLee Young-AeBeyer KirstenVölzke HenryPigeot IrisTraidl-Hoffmann ClaudiaDuijts LiesbethLu HaojieRaitakari Olli TLehtimäki TerhoKähönen MikaThio Chris H LMelén ErikPennell Craig EHolloway John Wvon Mutius ErikaSiroux ValérieBønnelykke KlausCustovic AdnanSimpson AngelaSchikowski TamaraBilbao Jose RamonSchaub BiancaPeters RachelKersten Elin T GVonk Judith MThiering ElisabethPeters AnnetteKoppelman Gerard HStandl Marie - Microtubule organization plays a central role in cell differentiation, orchestrating essential processes such as cell polarization, mechanotransduction, organelle positioning and intracellular transport. A hallmark of many differentiated cells is the transition from a centrosomal to a non-centrosomal microtubule-organizing center (MTOC). Here, we demonstrate that both centrosomal and nuclear envelope (NE)-associated MTOCs coexist in osteoclasts. We show that the key players for NE-MTOC formation, the AKAP6 and nesprin-1 (SYNE1) isoforms AKAP6β and nesprin-1α, previously considered muscle specific, are upregulated during osteoclast differentiation, suggesting a conserved role in NE-MTOC assembly across cell types. Targeted depletion of AKAP6 in RAW264.7-derived osteoclasts led to the displacement of the Golgi and MTOC-associated proteins PCM1, pericentrin and CDK5RAP2 from the NE, while their centrosomal localization remained intact. This selectively impaired microtubule nucleation from the NE without disrupting centrosomal microtubule activity, enabling a functional dissection of the two MTOCs. Loss of NE-MTOC activity, through AKAP6 depletion, impaired podosome formation and significantly reduced bone resorption capacity, highlighting the distinct and essential role of NE-derived microtubules in osteoclast function. - Source: PubMed
Publication date: 2026/01/23
Vergarajauregui SilviaPanea SamanthaOltmanns Jakob OSteffen UlrikeEngel Felix B