Journal of cell science最新文献_第7页

Accelerated organelle movements can indirectly affect the motility of other organelles in plant cells. 细胞器运动加速可以间接影响植物细胞中其他细胞器的运动。

IF 3.9 3区生物学

Journal of cell science Pub Date : 2026-09-15 Epub Date: 2026-09-25 DOI: 10.1242/jcs.264573

Jin-Mo Gu, Alex Keith, Kylie Smith, Andreas Nebenführ

{"title":"Accelerated organelle movements can indirectly affect the motility of other organelles in plant cells.","authors":"Jin-Mo Gu, Alex Keith, Kylie Smith, Andreas Nebenführ","doi":"10.1242/jcs.264573","DOIUrl":"10.1242/jcs.264573","url":null,"abstract":"Organelle movements in plants are driven by myosin XI motors moving along the actin filament cytoskeleton. Several experiments have suggested that indirect effects such as organelle-organelle interactions or hydrodynamic flow might be responsible for organelle movements. To test these models, we altered the motile behavior of specific organelles in Nicotiana benthamiana leaf epidermal cells and examined the effects of these perturbations on other organelles. Recruiting myosins to organelles with 'Booster' constructs resulted in significant increases of linear motions, whereas binding organelles to cortical microtubules with 'Anchor' constructs lead to diminished movements of the targeted mitochondria, peroxisomes and ER, respectively. We did not observe consistent effects of Anchor constructs on non-targeted organelles. Mitochondrial Boosters increased the motility of all tested organelles, presumably by leading to a reorganization of actin filaments. By contrast, ER Boosters resulted in enhanced movements for only Golgi stacks and peroxisomes, suggesting a specific interaction between these organelles. Collectively, this novel engineering approach to modify the movements of specific organelles demonstrates that organelle motility in plant cells can occur independently but nevertheless is coordinated between different types of organelles.","PeriodicalId":15227,"journal":{"name":"Journal of cell science","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13680970/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148808637","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The mechanisms and mechanics of aging. 衰老的机制和机制。

IF 3.9 3区生物学

Journal of cell science Pub Date : 2026-09-15 Epub Date: 2026-09-24 DOI: 10.1242/jcs.264835

Anastasia Zhurikhina, Maia Kirkegaard, Alberto Guarnieri, Hanna L Martens

{"title":"The mechanisms and mechanics of aging.","authors":"Anastasia Zhurikhina, Maia Kirkegaard, Alberto Guarnieri, Hanna L Martens","doi":"10.1242/jcs.264835","DOIUrl":"https://doi.org/10.1242/jcs.264835","url":null,"abstract":"Aging tissues paradoxically stiffen while losing mechanical resilience, becoming fragile, poorly regenerative and chronically inflamed. We review evidence that these phenotypes emerge from progressive failure of mechanotransduction across a mechanically integrated axis linking extracellular matrix (ECM) architecture, integrin adhesions, cytoskeletal force transmission and nuclear mechanics. We discuss how matrisome remodeling, glycation-driven crosslinking and reduced ECM turnover alter not only bulk stiffness but also fiber deformability, ligand presentation and matrix remodelability, thereby lowering the fidelity of mechanosensing. We then synthesize how distorted mechanical inputs and age-intrinsic changes in mechanotransduction machinery propagate through focal adhesion signaling, actin-microtubule dynamics, mechanosensitive ion channels and nucleo-cytoskeletal coupling to dysregulate mechanosensitive transcription factors (including YAP/TAZ and MRTF), promote senescence and amplify the senescence-associated secretory phenotype (SASP), which further degrades the ECM. Finally, we highlight premature aging syndromes as causal evidence showing that disruption of either ECM structure or nuclear integrity can collapse mechanotransductive homeostasis and trigger tissue degeneration. Together, these studies support a mechanical drift framework and motivate rejuvenation strategies aimed at resetting the aged mechanochemical niche.","PeriodicalId":15227,"journal":{"name":"Journal of cell science","volume":"139 18","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149038916","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The pyrenoid at a glance. 类pyrenoid的英文：

IF 3.9 3区生物学

Journal of cell science Pub Date : 2026-09-15 Epub Date: 2026-09-28 DOI: 10.1242/jcs.264787

Philippe Van der Stappen, Benjamin D Engel, Manon Demulder

引用次数: 0

CCT8 associates with the MYO10 motor domain and regulates filopodia and breast cancer cell invasion. CCT8与MYO10运动结构域相关，调控丝状足和乳腺癌细胞侵袭。

IF 3.9 3区生物学

Journal of cell science Pub Date : 2026-09-15 Epub Date: 2026-09-29 DOI: 10.1242/jcs.265278

Ana Popović, Marjaana Ojalill, Christine Touma, Neil J Ball, Mitro Miihkinen, Omkar Joshi, Michal Dibus, Joanna Pylvänäinen, Johanna Ivaska, Benjamin T Goult, Guillaume Jacquemet

{"title":"CCT8 associates with the MYO10 motor domain and regulates filopodia and breast cancer cell invasion.","authors":"Ana Popović, Marjaana Ojalill, Christine Touma, Neil J Ball, Mitro Miihkinen, Omkar Joshi, Michal Dibus, Joanna Pylvänäinen, Johanna Ivaska, Benjamin T Goult, Guillaume Jacquemet","doi":"10.1242/jcs.265278","DOIUrl":"10.1242/jcs.265278","url":null,"abstract":"Cancer cells utilize filopodia to explore, adhere to and invade their surrounding microenvironment, yet the protein networks that organize these protrusions remain incompletely defined. To uncover the molecular machinery underlying MYO10-positive filopodia, we targeted the fast biotin ligase TurboID to the motor protein MYO10. Proximity biotinylation in two cell types revealed hundreds of potential MYO10 interactors. A targeted microscopy and siRNA screen identified MINK1, SCRIB, CSNK1A1 and CCT8 as new regulators of MYO10-mediated filopodia formation. Focusing on one of the interactors shared between cell lines, CCT8, known as a subunit of the chaperonin TCP1 ring complex (TRiC), we found that CCT8 associates with the MYO10 motor domain and regulates MYO10 filopodia independently of the TRiC. Depleting CCT8 affected filopodia dynamics and impaired cell spreading, migration and invasion in breast cancer cells. These findings establish CCT8 as a TRiC-independent regulator of MYO10 filopodia across diverse cancer cell types.","PeriodicalId":15227,"journal":{"name":"Journal of cell science","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13676896/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148864125","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Atypical PI3Ks coordinate chemotaxis, signaling dynamics and multicellular development in Dictyostelium. 非典型pi3k协调盘基骨的趋化性、信号动力学和多细胞发育。

IF 3.9 3区生物学

Journal of cell science Pub Date : 2026-09-15 Epub Date: 2026-10-02 DOI: 10.1242/jcs.265041

Laith Bahlouli, Erik Zhang, Eric Jung, Taylor Brentjens, Elizabeth A Rose, Harrison Drebin, Benjamin Edwards, Isabella Wischik, Alyssa B Huynh, William Callahan, Jacqueline M Shen, Susanna Li, Kevin Zhangxu, Marc Edwards

{"title":"Atypical PI3Ks coordinate chemotaxis, signaling dynamics and multicellular development in Dictyostelium.","authors":"Laith Bahlouli, Erik Zhang, Eric Jung, Taylor Brentjens, Elizabeth A Rose, Harrison Drebin, Benjamin Edwards, Isabella Wischik, Alyssa B Huynh, William Callahan, Jacqueline M Shen, Susanna Li, Kevin Zhangxu, Marc Edwards","doi":"10.1242/jcs.265041","DOIUrl":"10.1242/jcs.265041","url":null,"abstract":"Phosphoinositide 3-kinase (PI3K) signaling regulates protrusion, polarity, membrane uptake and multicellular development in Dictyostelium discoideum, but these functions have been interpreted largely through canonical class I PI3Ks and phosphatidylinositol (3,4,5)-trisphosphate [PI(3,4,5)P3] production. This framework does not fully explain how PI3K-dependent pathways restrain Ras activity, organize relay signaling or coordinate the transition from single-cell migration to multicellular aggregation. Here, we show that three atypical PI3K-family enzymes, PikF, PikG and PikH, define genetically separable functions within this broader PI3K signaling network. PikF attenuates Ras-phosphoinositide-actin signaling, limiting protrusive activity so that chemotactic responses remain spatially and temporally constrained. PikG is required for aggregation and supports adenylyl cyclase A-dependent cAMP relay, coupling cellular polarity to the collective signaling needed for streaming and multicellular development. PikH separates uptake from these chemotactic and developmental functions by supporting efficient phagocytosis, with little effect on acute cAMP-stimulated signaling. Together, these findings expand the Dictyostelium PI3K framework beyond a class I PI(3,4,5)P3-centered pathway and identify atypical PI3Ks as specialized regulators of signal attenuation, cAMP relay organization and membrane uptake.","PeriodicalId":15227,"journal":{"name":"Journal of cell science","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13676897/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148828684","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Analysis of motor-based transport in primary cilia by dynamic mode decomposition of live-cell imaging data. 利用活细胞成像数据的动态模态分解分析初级纤毛的运动传输。

IF 3.9 3区生物学

Journal of cell science Pub Date : 2026-09-15 DOI: 10.1242/jcs.264918

Fabiola Campestre, Line Lauritsen, Lotte B Pedersen, Daniel Wüstner

{"title":"Analysis of motor-based transport in primary cilia by dynamic mode decomposition of live-cell imaging data.","authors":"Fabiola Campestre, Line Lauritsen, Lotte B Pedersen, Daniel Wüstner","doi":"10.1242/jcs.264918","DOIUrl":"https://doi.org/10.1242/jcs.264918","url":null,"abstract":"Kinesin-3 motor proteins are increasingly recognized for their important roles in cilia. The mammalian kinesin-3 motor KIF13B moves bidirectionally in primary cilia and regulates ciliary content, but its relationship to the intraflagellar transport (IFT) machinery is unclear. Here, we combine quantitative live-cell imaging with a new kymograph analysis based on dynamic mode decomposition (DMD) to separate mobile from immobile protein populations in primary cilia. This approach simplifies extraction of molecular velocities from kymographs and improves directional analysis of molecular tracks using the Fourier and Radon transforms. Our novel analysis reveals that a KIF13B deletion mutant retaining only the motor domain and part of the forkhead-associated domain does not alter steady-state IFT velocity or frequency. However, when retrograde dynein-2 function is inhibited by Ciliobrevin D or Tanespimycin, both anterograde and retrograde IFT velocities decrease in parental cells, as expected, but remain unchanged in KIF13B mutant cells. Structured illumination, confocal, and STED microscopy further show that KIF13B localizes to the ciliary membrane and concentrates at the periciliary membrane region and the centriolar subdistal appendages, below the distal appendage marker FBF1. Our improved kymograph approach provides new insight into KIF13B ciliary function and simplifies the quantitative analysis of ciliary protein transport.","PeriodicalId":15227,"journal":{"name":"Journal of cell science","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148968838","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Exposure of cells to prions induces prion strain-dependent changes in mitochondrial redox state and respiration. 细胞暴露于朊病毒诱导朊病毒菌株依赖的线粒体氧化还原状态和呼吸变化。

IF 3.9 3区生物学

Journal of cell science Pub Date : 2026-09-15 Epub Date: 2026-09-25 DOI: 10.1242/jcs.264762

Daniel Shoup, Leah R Varner, Brent Race, Elyssa Hawk, Suzette A Priola

{"title":"Exposure of cells to prions induces prion strain-dependent changes in mitochondrial redox state and respiration.","authors":"Daniel Shoup, Leah R Varner, Brent Race, Elyssa Hawk, Suzette A Priola","doi":"10.1242/jcs.264762","DOIUrl":"10.1242/jcs.264762","url":null,"abstract":"Prion diseases are transmissible, neurodegenerative diseases caused by misfolded, protease-resistant and infectious aggregates of the mammalian prion protein (PrPSc) that replicate by converting properly folded prion protein (PrPC, encoded by PRNP in humans) into PrPSc. Spongiform change and cellular loss in the brain are hallmarks of prion disease, but our understanding of how prions alter cellular fitness remains incomplete. Here, we characterized changes in mitochondrial redox state and respiration in mouse neural cells following uptake of two different PrPSc strains: 22L and 87V. Only 22L PrPSc induced changes in cellular respiration and mitochondrial redox state, even in cells that did not produce PrPC. These effects were disrupted by treatment with detergent and dependent upon endolysosomal acidification, suggesting that both PrPSc membrane association and lysosomal degradation are involved. Interestingly, cells chronically infected with 22L appeared to adapt to infection, showing no signs of mitochondrial dysfunction, but were more susceptible to oxidative stress even though mitochondrial respiration was normal. Thus, during initial prion infection, PrPSc drives mitochondrial dysfunction in a manner that is both strain dependent and independent of PrPC expression, whereas persistent prion infection increases mitochondrial sensitivity to cellular stress.","PeriodicalId":15227,"journal":{"name":"Journal of cell science","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13680968/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148864146","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Localized disruption of the presynaptic endoplasmic reticulum in Atlastin mutants. 阿联素突变体突触前内质网的局部破坏。

IF 3.9 3区生物学

Journal of cell science Pub Date : 2026-09-14 DOI: 10.1242/jcs.265223

Mónica C Quiñones-Frías, Dina M Ocken, Avital A Rodal

{"title":"Localized disruption of the presynaptic endoplasmic reticulum in Atlastin mutants.","authors":"Mónica C Quiñones-Frías, Dina M Ocken, Avital A Rodal","doi":"10.1242/jcs.265223","DOIUrl":"10.1242/jcs.265223","url":null,"abstract":"The endoplasmic reticulum (ER) extends throughout neurons and regulates many functions, including neurite outgrowth, neurotransmission, and synaptic plasticity. Mutations in ER-shaping proteins cause the neurodegenerative disorder Hereditary Spastic Paraplegia (HSP), yet the ultrastructure and dynamics of neuronal ER remain largely unexplored, especially at presynaptic terminals. Using super-resolution and live imaging in Drosophila larval motor neurons, we investigated ER structure in wild-type animals and mutants of the HSP-linked gene, Atlastin, which encodes an ER-shaping protein. Previous studies reported diffuse localization of an ER luminal marker at Atlastin mutant presynaptic terminals, which was attributed to ER fragmentation. Using an ER membrane marker, we found that Atlastin mutant ER forms robust networks with only mild defects in structure and dynamics, indicating that the primary defect is functional rather than architectural. We demonstrate that Atlastin mutants progressively displace a luminal ER protein reporter to the cytosol during larval development, specifically at synapses, while this reporter remains correctly localized in cell bodies, axons, and muscles. This synapse-specific displacement phenotype, previously unreported in non-neuronal cells, emphasizes the importance of studying neurons to understand HSP pathogenesis.","PeriodicalId":15227,"journal":{"name":"Journal of cell science","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148963311","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

DHHC21 is a STIM1 protein S-acyltransferase that modulates immune function in vivo. DHHC21是体内调节免疫功能的STIM1蛋白s -酰基转移酶。

IF 3.9 3区生物学

Journal of cell science Pub Date : 2026-09-01 Epub Date: 2026-09-11 DOI: 10.1242/jcs.264681

Goutham Kodakandla, Ying Fan, Michael X Zhu, Savannah J West, Askar Akimzhanov, Darren Boehning

{"title":"DHHC21 is a STIM1 protein S-acyltransferase that modulates immune function in vivo.","authors":"Goutham Kodakandla, Ying Fan, Michael X Zhu, Savannah J West, Askar Akimzhanov, Darren Boehning","doi":"10.1242/jcs.264681","DOIUrl":"10.1242/jcs.264681","url":null,"abstract":"Depletion of Ca2+ from ER stores leads to the activation of Ca2+ channels on the plasma membrane known as store-operated Ca2+ entry. The proteins STIM1 and STIM2 function as ER Ca2+ sensors, and upon store depletion, they undergo a conformational change that allows them to bind to and gate Orai Ca2+ channels on the plasma membrane. We have shown that both Orai1 and STIM1 are dynamically S-acylated after store depletion, which is required for SOCE. These results suggest the requirement of a Ca2+-activated protein S-acyltransferase (PAT) such as DHHC21 (also known as zDHHC21). Here, we show that DHHC21 is essential for SOCE in vitro and in vivo. Using the depilated mouse model, which expresses DHHC21 that cannot be activated by Ca2+, we show that DHHC21 activation is a major mediator of STIM1 S-acylation and subsequent Ca2+ entry. Plasma membrane-localized DHHC21 is dynamically recruited into Orai1-STIM1 puncta upon store depletion, where it physically binds to STIM1. Finally, we show that depilated mice phenocopy many aspects of autoimmune lymphoproliferative syndrome (ALPS), including defective Fas-mediated Ca2+ release, T cell death, neutropenia and increased serum vitamin B12 levels. Targeting DHHC21 might be therapeutically beneficial for ALPS and diseases associated with deregulated activation of STIM1, such as tubular aggregate myopathy and Stormorken syndrome.","PeriodicalId":15227,"journal":{"name":"Journal of cell science","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13615677/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148760570","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Phosphorylation of the AP2 μ2 subunit by p70S6 kinase facilitates clathrin-mediated endocytosis. p70S6激酶磷酸化AP2µ2亚基促进网格蛋白介导的内吞作用。

IF 3.9 3区生物学

Journal of cell science Pub Date : 2026-09-01 Epub Date: 2026-09-10 DOI: 10.1242/jcs.264867

Aleksandra Tempes, Agnieszka Brzozowska, Tomasz Węgierski, Ayomide Fasemire, Katarzyna Olek, Kamil Jastrzębski, Ewa Liszewska, Katarzyna Misztal, Katarzyna Machnicka, Matylda Macias, Aleksandra Szybińska, Ewa Sitkiewicz, Agata Malinowska, Agata Gozdz, Agnieszka Wyszyńska, Anna Łasica, Marta Hoffmann-Młodzianowska, Katarzyna Orzoł, Marta Miączyńska, Maria W Górna, Wojciech Pokrzywa, Jacek Jaworski, Anna R Malik

{"title":"Phosphorylation of the AP2 μ2 subunit by p70S6 kinase facilitates clathrin-mediated endocytosis.","authors":"Aleksandra Tempes, Agnieszka Brzozowska, Tomasz Węgierski, Ayomide Fasemire, Katarzyna Olek, Kamil Jastrzębski, Ewa Liszewska, Katarzyna Misztal, Katarzyna Machnicka, Matylda Macias, Aleksandra Szybińska, Ewa Sitkiewicz, Agata Malinowska, Agata Gozdz, Agnieszka Wyszyńska, Anna Łasica, Marta Hoffmann-Młodzianowska, Katarzyna Orzoł, Marta Miączyńska, Maria W Górna, Wojciech Pokrzywa, Jacek Jaworski, Anna R Malik","doi":"10.1242/jcs.264867","DOIUrl":"10.1242/jcs.264867","url":null,"abstract":"Clathrin-mediated endocytosis (CME) internalizes cell-surface receptors via clathrin-coated invaginations of the plasma membrane. Both clathrin and endocytic cargo are recruited to these sites by the adaptor protein complex AP2. AP2 cycles between a closed cytoplasmic conformation and an open membrane-bound state, and efficient CME requires both conformations and their dynamic interconversion. The mechanisms regulating these conformational changes, which include post-translational modifications of the AP2, remain incompletely understood. Here, we report that, in human cell lines, p70S6 kinase phosphorylates the μ2 subunit of the AP2 and that the phosphorylation of serine 45 (S45) depends on p70S6K activity. Loss of S45-μ2 phosphorylation results in decreased internalization of canonical CME cargo, such as transferrin and PDGF receptors. In Caenorhabditis elegans, lack of S45-μ2 phosphorylation produces directionally similar but markedly weaker phenotypes than AP2 loss of function. Live imaging and computational dynamic modelling suggest that S45-μ2 phosphorylation has an impact on the conformational changes of the AP2 complex. These findings identify a p70S6K-dependent mechanism that modulates AP2 function and further strengthen the importance of post-translational regulation in controlling CME.","PeriodicalId":15227,"journal":{"name":"Journal of cell science","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148630570","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0