Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1038/s42003-025-09229-8 http://scihub22266oqcxt.onion/10.1038/s42003-025-09229-8 41366027!?!41366027 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=41366027&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Commun+Biol 2025 ; ? (?): ? Nephropedia Template TP {{tp|p=41366027|t=2025. Elevated SUN1 promotes migratory cell polarity defects through mechanically coupling microtubules to the nuclear lamina |pdf=|usr=}}{{41366027}} gab.com Text Elevated SUN1 promotes migratory cell polarity defects through mechanically coupling microtubules to the nuclear lamina JO: Commun Biol http://www.kidney.de/pget.php?&tw=1&pmid=41366027 #FOAvip In migratory fibroblasts, front-rear polarity is defined by the centrosome positioned anterior to a rearward nucleus. To achieve this polarity, actin cables couple to nuclear membrane proteins nesprin-2G and SUN2 and drive the nucleus backward. Aging disrupts this polarity by increasing SUN1, a SUN2 homolog. Here, we investigated the molecular mechanisms behind this disruption and found that the dominant-negative effect of SUN1 and progerin, a lamin A variant, required direct SUN1-lamin A interaction. Microtubule interaction and force transmission through a nesprin, identified as nesprin-2, are crucial for SUN1's effect. We further discovered that stable microtubules are both necessary and sufficient to inhibit cell polarity. Using SUN1-SUN2 chimeric proteins, we demonstrated that the SUN domains determine their roles in cell polarization. Our findings reveal how elevated SUN1 disrupts cell polarity through coupling microtubules and nuclear lamina, emphasizing the impact of altered microtubule stability and nuclear mechanotransduction in polarity defects. Twit Text FOAVip Elevated SUN1 promotes migratory cell polarity defects through mechanically coupling microtubules to the nuclear lamina ????Commun Biol http://www.kidney.de/pget.php?&tw=1&pmid=41366027 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=41366027 #FOAvip English Wikipedia <ref>{{Cite pmid|41366027}}</ref> Elevated SUN1 promotes migratory cell polarity defects through mechanically coupling microtubules to the nuclear lamina #MMPMID41366027 Li Y; Zhang Y; Chen M; Antoku S; Ding J; Huang K; Gundersen GG; Chang W Commun Biol 2025[Dec]; ? (?): ? PMID41366027show ga In migratory fibroblasts, front-rear polarity is defined by the centrosome positioned anterior to a rearward nucleus. To achieve this polarity, actin cables couple to nuclear membrane proteins nesprin-2G and SUN2 and drive the nucleus backward. Aging disrupts this polarity by increasing SUN1, a SUN2 homolog. Here, we investigated the molecular mechanisms behind this disruption and found that the dominant-negative effect of SUN1 and progerin, a lamin A variant, required direct SUN1-lamin A interaction. Microtubule interaction and force transmission through a nesprin, identified as nesprin-2, are crucial for SUN1's effect. We further discovered that stable microtubules are both necessary and sufficient to inhibit cell polarity. Using SUN1-SUN2 chimeric proteins, we demonstrated that the SUN domains determine their roles in cell polarization. Our findings reveal how elevated SUN1 disrupts cell polarity through coupling microtubules and nuclear lamina, emphasizing the impact of altered microtubule stability and nuclear mechanotransduction in polarity defects. ?Elevated SUN1 promotes migratory cell polarity defects through mechani(epmc).pdf DeepDyve Pubget Overpricing