Ask about this productRelated genes to: SH3KBP1 antibody
- Gene:
- SH3KBP1 NIH gene
- Name:
- SH3 domain containing kinase binding protein 1
- Previous symbol:
- -
- Synonyms:
- CIN85
- Chromosome:
- Xp22.12
- Locus Type:
- gene with protein product
- Date approved:
- 2000-12-14
- Date modifiied:
- 2016-10-05
Related products to: SH3KBP1 antibody
Related articles to: SH3KBP1 antibody
- Ovarian cancer (OC) remains the most lethal gynecological malignancy, with profound tumor microenvironment (TME) heterogeneity contributing to the suboptimal clinical response to immune checkpoint inhibitors (ICIs). Therefore, delineating the metabolic heterogeneity of T cells within the TME is imperative for identifying precise prognostic biomarkers and refining individualized immunotherapeutic strategies. - Source: PubMed
Publication date: 2026/04/24
Tian HuadongLiu XiaotongWang GuojiaoWang ZimoLuo Yuexi - Aberrant lipid metabolism is a hallmark of hepatocellular carcinoma (HCC), yet the regulatory mechanisms governing lipid droplet (LD) dynamics and their contribution to tumor progression remain poorly understood. Here, we developed an ultrasensitive phosphoproteomic platform using high-affinity HPDA@Ti nanospheres to map LD-associated phosphorylation events across six HCC cell lines. By correlating phosphoproteomic signatures with LD morphology, we identified distinct regulatory signatures associated with LD size and abundance. Functional perturbation screens identified two distinct phosphoprotein modules controlling LD size: silencing , , , , and reduced LD size in Huh1 cells, whereas silencing , , , , , and enlarged LDs in Huh7 cells. Notably, we identified EPB41L3 as a critical metabolic-metastatic link; its loss decreased LD size and accelerated HCC migration and invasion, correlating with poor clinical prognosis. Crucially, we identified five key phosphorylation sites on EPB41L3 essential for its function; substituting these with alanine completely abolished its regulatory control over both LD size and HCC metastatic potential. Together, these findings delineate a phosphorylation-based regulatory network controlling the LD architecture and metastatic potential in HCC. Our study not only identifies potential therapeutic targets but also establishes a generalizable phosphoproteomic framework for interrogating lipid signaling in cancer metabolism. - Source: PubMed
Publication date: 2026/05/29
Mao Jian-WenXia YanLuo Xue-YangWang ShupeiGong JingyiXu JindianChen WeiweiWu JiaqiLi ZimengLuo JiahuiZhang HongyeLu QingWu DuojiaoWu Wei-ZhongWang JiaxiHuang Li-Hao - USP8 is one of the members of ubiquitin-specific proteases deconjugating ubiquitin from target proteins. Besides USP6, it can be involved in tumorigenesis of mesenchymal neoplasms by binding to an activating fusion partner. Until now, USP8 fusion genes have been reported in calcified chondroid mesenchymal neoplasms, an inflammatory myofibroblastic tumor, a cardiac neoplasm, and a retroperitoneal sarcoma. In this study, we describe the clinicopathologic and genetic/epigenetic features of 7 USP8-associated tumors. The cohort included 5 male patients aged between 2 and 11 years, and 2 female patients aged 38 and 52 years. Lesions arose in the tongue, finger, hallux, arm, thoracic wall, right ventricle, and leg. Five neoplasms were resected. One was a recent case; the others were without evidence of disease after 0.5 to 3 years. Two lesions were only biopsied, 1 was a recent case and the other had no signs of progression after 4 years. Histology showed nodular or infiltrative lesions comprising bland-looking myofibroblastic spindle cells arranged in mainly short fascicles. The cellularity was variable, and the background was myxoid and/or collagenous. An inflammatory reaction was variably seen. One lesion, however, had features of a chondroid calcified mesenchymal neoplasm. Using RNA-sequencing, the following fusion partners of USP8 were found: SH3KBP1, RASA1, PDGFRA, CRK, PTPN11, and FARP1. Based on RNA-expression analysis, the 2 cases analyzed had a profile of nodular fasciitis; whereas using the Heidelberg Sarcoma Classifier, all cases had a similar methylation profile apart from other soft tissue tumor entities, suggesting that they form a separate group but are closely related to USP6-associated lesions. In conclusion, we broadened the spectrum of USP8-associated mesenchymal lesions in superficial, deep soft tissues and viscera (heart). Almost all lesions in this series displayed a myofibroblastic phenotype and harbored variable USP8 fusion partners. RNA-expression profiling indicated partial clustering with nodular fasciitis, suggesting some biological similarity. However, DNA methylation analysis consistently showed that these tumors formed a distinct epigenetic group, separate from both nodular fasciitis and inflammatory myofibroblastic tumors. Taken together, these findings support the concept of a USP8-rearranged myofibroblastic neoplasm as a potentially distinct entity, but the precise relationship with nodular fasciitis and inflammatory myofibroblastic tumor remains uncertain. Further studies integrating morphology, epigenetics, and transcriptomics are needed to clarify this relationship. - Source: PubMed
Publication date: 2025/12/09
Arciuolo DamianoBarresi SabinaHiemcke-Jiwa LauraBlack JenniferWillard NicholasCarta RobertoRoe MichelleBukowinski AndrewStracuzzi AlessandraKester LennartKoudijs MarcoDingemans WillemijnMilano Giuseppe MariaPatrizi SaraGestrich CatherineJohn IvyAzfar NeyazBubar RobertSkaugen JohnFlucke UtaMiele EvelinaAlaggio Rita - Pancreatic ductal adenocarcinoma (PDAC) is among the most aggressive malignancies with extremely poor prognosis. This study systematically evaluates the expression patterns, biological functions, and regulatory mechanisms of the SH3-domain kinase binding protein 1 (SH3KBP1) in PDAC through multi-omics integrative analysis strategies. - Source: PubMed
Publication date: 2025/10/31
Sun Rui ZhuangQiao Kun PengXu Xiao LianChen Yan HuaMeng Jun - MYO1F, a long-tailed myosin of class I, is selectively expressed in immune cells and upregulated in microglia associated with neurodegenerative pathogenesis. Myosin motor functions are regulated by adaptor proteins that mediate cargo attachment and motor recruitment. To define the MYO1F interactome, we used in situ proximity labelling and proteomics in human myeloid cells. We identified a distinct SH3-domain-dependent adaptor module comprising CD2AP, ASAP1, SH3BP2 and SH3KBP1 (herein termed the CASS group of proteins). Interestingly, CD2AP is an Alzheimer's disease (AD) risk gene upregulated in the microglia of individuals with AD, which are implicated in phagocytic responses to amyloid-β. Structural modelling and mutagenesis confirmed multivalent proline-rich motif interactions between the CASS group of proteins and the MYO1F SH3 domain. Additional binding partners associate with the MYO1F pleckstrin homology (PH) domain. Immunofluorescence revealed colocalisation of MYO1F and the CASS group of proteins at actin-rich podosomes and phagocytic cups in macrophages and microglia. Functional assays demonstrated that MYO1F recruitment to the phagocytic cup requires motor activity and intact PH and SH3 domains. We provide the first MYO1F interactome identifying adaptor proteins for MYO1F in podosomes and during phagocytosis, offering new insights into its function in disease-associated microglia during neurodegeneration. - Source: PubMed
Publication date: 2025/12/22
Arden Susan DPennink EvaLakatos AndrásGriffiths Gillian MLippert Anna HBuss Folma