PPFIA1 Antibody
- Known as:
- PPFIA1 Antibody
- Catalog number:
- XW-7817
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- PPFIA1 Antibody
Related genes to: PPFIA1 Antibody
- Gene:
- PPFIA1 NIH gene
- Name:
- PTPRF interacting protein alpha 1
- Previous symbol:
- -
- Synonyms:
- LIP.1, LIPRIN
- Chromosome:
- 11q13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-23
- Date modifiied:
- 2016-02-10
Related products to: PPFIA1 Antibody
Related articles to: PPFIA1 Antibody
- Colorectal cancer (CRC) remains the second leading cause of cancer mortality in the U.S., with significant racial and ethnic disparities in incidence, survival, and mortality rates. The rising incidence of early-onset CRC and the frequent presentation at advanced stages of CRC among the Hispanics makes this an important ethnic group to study. A deeper understanding of the complex interplay between molecular, genetic, and environmental factors is critical for developing targeted therapies to reduce the prevalence in specific racial and ethnic groups, such as Hispanics. This study explores the role of stress-survival pathway (SSP) genes in early-onset and late-stage CRC, primarily focusing on disparities between Hispanics and Non-Hispanic Whites (NHWs). Additionally, this study investigates the role of MCM10, in contributing to CRC disparities among the Hispanic populations with an emphasis of early-onset and late-stage CRC Hispanics. - Source: PubMed
Publication date: 2026/01/07
Islam Khan Md ZahirulBasnet UrbashiNair SoumyaKulkarni AditiRangel Frances ATorres AngelBasu AnamikaAlmeida Igor CAl-Hilal TaslimRoy Sourav - A dynamic protein network at the leading edge of motile cells is needed to coordinate events required for efficient cell motility. Previous work has shown that the Ser/Thr kinase DYRK3 affects the assembly of this network, and phosphorylates its component Liprin-α1, a scaffold protein regulating adhesion turnover and cell motility. We have looked for phospho-sites of Liprin-α1 relevant for the regulation of cell motility, by examining the role played by serine/threonine residues phosphorylated within the intrinsically disordered regions of Liprin-α1. Phospho-null mutations within either the amino-terminal or the carboxy-terminal disordered regions affect Liprin-α1 phosphorylation induced by DYRK3. Functional analysis shows that mutations within the amino-terminal region do not affect cell motility, while a set of carboxy-terminal mutations reduces the positive effects of Liprin-α1 on cell spreading on the extracellular matrix. Among several candidate phospho-sites in this protein region, we identify Thr701 as one of the potential main targets of DYRK3 activity in Liprin-α1. The phospho-null mutation of Thr701 specifically inhibits Liprin-α1-induced potentiation of cell spreading on fibronectin. Our findings contribute to highlight the complexity of the regulation of Liprin-αprotein functions by phosphorylation/dephosphorylation events. Given the involvement of Liprin-α proteins in tumor cell motility and invasion, in-depth understanding of this regulatory complexity may highlight new possibilities for therapeutic intervention. - Source: PubMed
Publication date: 2025/12/01
Ramella MartinaBrambilla DanieleSurini SaraTonoli DilettaRibolla Lucrezia Mariade Curtis Ivan - Cisplatin resistance remains a significant challenge in treating lung squamous cell carcinoma (LUSC). The role of FADD in this resistance requires further investigation. Our study revealed that FADD is overexpressed in LUSC patients, correlating with lower survival rates. We also discovered that long-term cisplatin-resistant LUSC cell lines (LUSC-CR) had elevated FADD protein levels, and reducing FADD restored their cisplatin sensitivity. At the same time, LUSC-CR cells resisted cisplatin-induced DNA damage and had enhanced DNA repair, linked to P53's negative regulation of FADD. Additionally, knockdown of the long non-coding RNA (lncRNA) PPFIA1-AS1 can potentiate drug resistance in LUSC cells by decelerating FADD protein turnover and elevating FADD protein levels. In essence, this study elucidated novel mechanisms underlying cisplatin resistance in LUSC, wherein the PPFIA1-AS1/FADD axis regulates DNA damage and repair. Consequently, targeting the PPFIA1-AS1/FADD axis may present a promising avenue for overcoming cisplatin resistance and enhancing the prognosis of LUSC patients. - Source: PubMed
Publication date: 2025/11/14
Chang XiaoyaoLi DangranTan YuanhaoCai FangfangFu ShuilianZhuang HongqinHua Zi-Chun - Presynaptic scaffold proteins, including liprin-α, RIM, and ELKS, are pivotal to the assembly of the active zone and regulating the coupling of calcium signals and neurotransmitter release, yet the underlying mechanism remains poorly understood. Here, we determined the crystal structure of the liprin-α2/RIM1 complex, revealing a multifaceted intermolecular interaction that drives the liprin-α/RIM assembly. Neurodevelopmental disease-associated mutations block the formation of the complex. Disrupting this interaction in cultured human neurons impairs synaptic transmission and reduces the readily releasable pool of synaptic vesicles. Super-resolution imaging analysis supports a role for liprin-α in recruiting RIM1 to the active zone, presumably by promoting the liquid-liquid phase separation (LLPS) of RIM1. Strikingly, the liprin-α/RIM interaction modulates the competitive distribution of ELKS1 and voltage-gated Ca2+ channels (VGCCs) in RIM1 condensates. Disrupting the liprin-α/RIM interaction significantly decreased VGCC accumulation in the condensed phase and rendered release more sensitive to the slow calcium buffer EGTA, suggesting an increased physical distance between VGCC and vesicular calcium sensors. Together, our findings provide a plausible mechanism of the liprin-α/RIM complex in regulating the coupling of calcium channels and primed synaptic vesicles via LLPS for efficient synaptic transmission and uncover the pathological implication of liprin-α mutations in neurodevelopmental disorders. - Source: PubMed
Publication date: 2025/06/10
Jin GaoweiCampos JoaquínLiu Yangde la Cruz Berta MarcóZhang ShujingLiang MingfuLi KaiyueXie XingqiaoSterky Fredrik HAcuna ClaudioWei Zhiyi - Up to 80% of survivors of head and neck squamous cell carcinoma (HNSCC) currently or previously smoked. Thus, tobacco use is a major modifiable risk factor for HNSCC, even in the era of human papillomavirus (HPV)-associated disease. However, how smoking underlies chromosomal and epigenetic changes that are associated with HNSCC outcomes remains unclear. - Source: PubMed
Jiang RongGao May ZChen MengWeatherspoon Darien JWatts Tammara LOsazuwa-Peters Nosayaba