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X-WR-CALNAME:Biomolecular Sciences Seminar Series - Dr. Gant Luxton
X-WR-TIMEZONE:Mountain Time (US & Canada)
BEGIN:VEVENT
DTSTAMP:20260906T115841Z
UID:tag:localist.com\,2008:EventInstance_51782230943968
DTSTART:20260204T220000Z
DTEND:20260204T231500Z
DESCRIPTION:Biomolecular Sciences Seminar Series\n\nDr. Gant Luxton\, Unive
 rsity of California\, Davis\n\nTitle: Nuclear Envelope Proteins Control Cy
 toplasmic Mechanics Through Organelles and Ribosomal Axes Disrupted in Agi
 ng and Disease\n\nAbstract: Nuclear envelope proteins do far more than anc
 hor the nucleus\; they organize the cytoplasm. Using genetically encoded m
 ultimeric nanoparticles (GEMs) for passive nanorheology in living Caenorha
 bditis elegans\, we discovered that GEMs diffuse ~10-fold more slowly in t
 issue cytoplasm than cultured yeast or mammalian cells\, prompting us to a
 sk what establishes this mechanical environment in vivo. Building a GEM-ba
 sed tissue atlas across neurons\, muscle\, intestine\, hypodermis\, and ge
 rmline revealed that each tissue maintains a distinct biophysical signatur
 e and we identified two independent mechanisms controlling these differenc
 es. First\, ribosomes control macromolecular crowding. Second\, the giant 
 KASH protein ANC-1 (nesprin-1/2 ortholog) establishes cytoplasmic constrai
 nt through a LINC complex-independent function. ANC-1 also controls the po
 sitioning of ER\, mitochondria\, and lipid droplets\, as well as ER and mi
 tochondrial morphology. These two axes are separable: ribosomal crowding a
 nd organellar constraint can be independently tuned\, providing cells with
  distinct mechanisms for adjusting their mechano-metabolic environment. Nu
 clear lamins connect to this framework through ribosome biogenesis. Emery 
 Dreifuss muscular dystrophy-associatedlmn-1 mutations (R64P\, Y59C) disrup
 t nucleolar density\, reduce ribosome abundance\, and collapse ER architec
 ture\, phenocopying ribosome depletion and establishing a nucleolar-riboso
 mal axis through which nuclear lamina defects propagate to cytoplasmic dis
 organization\, providing a mechanistic basis for metabolic dysfunction in 
 muscular dystrophy. Importantly\, these mechano-metabolic axes deteriorate
  during physiological aging. Wild-type intestinal cytoplasm undergoes a dr
 amatic mechanical transition at day 9 that correlates with motility declin
 e and loss of ANC-1 accelerates this trajectory\; mutants exhibit “aged
 ” cytoplasmic mechanics from day 1\, progressive functional decline\, an
 d shortened lifespan. Domain analysis reveals that actin-binding and spect
 rin-repeat domains govern longevity\, while the transmembrane domain contr
 ols mechanics\, demonstrating separable but essential functions. Together\
 , our findings establish nuclear envelope proteins as mechano-metabolic in
 tegrators whose dysfunction drives both age-related decline and disease pa
 thogenesis.\n\nHost: Dr. Konrad Meister\, Department of Chemistry and Bioc
 hemistry
GEO:43.606007;-116.206294
LOCATION:Education Building (EDUC)\, 109
SUMMARY:Biomolecular Sciences Seminar Series - Dr. Gant Luxton
URL;VALUE=URI:https://events.boisestate.edu/event/biomolecular-sciences-sem
 inar-series-dr-gant-luxton
CATEGORIES:Lectures and Presentations
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