transparent gif


Ej inloggad.

Göteborgs universitets publikationer

Subunits of the chaperonin CCT interact with F-actin and influence cell shape and cytoskeletal assembly

Författare och institution:
Karen I. Brackley (Institutionen för cell- och molekylärbiologi, molekylärbiologi); Julie Grantham (Institutionen för cell- och molekylärbiologi, molekylärbiologi)
Publicerad i:
Experimental Cell Research, 316 ( 4 ) s. 543-553
Artikel, refereegranskad vetenskaplig
Sammanfattning (abstract):
The integrity of the cytoskeleton is closely linked to the oligomeric chaperonin containing TCP-1 (CCT) via the folding requirements of actin and tubulin, but the role of CCT in cytoskeletal organization remains unclear. We address this issue by analyzing the effects of targeting CCT subunits via siRNA and assessing their location/assembly state in cultured mammalian cells. Reducing levels of individual CCT subunits implicates CCTepsilon in influencing cell shape and reduced levels of this subunit limit the cells' ability to recover from microfilament depolymerization. Conversely, cells displayed enhanced microtubule regrowth when CCT subunit levels were altered by siRNA. Some CCT subunits co-localize with F-actin, whilst all are predominantly monomeric in extracts enriched for the cytoskeleton. This provides compelling evidence that some CCT subunits as monomers can influence cytoskeletal organization/polymerization. Therefore the activity of CCT may well extend beyond the folding of newly synthesized polypeptides, representing a novel function for CCT subunits distinct from their role in the CCT oligomer.
Ämne (baseras på Högskoleverkets indelning av forskningsämnen):
Biologiska vetenskaper ->
Biokemi och molekylärbiologi ->
Cell- och molekylärbiologi
Biologiska vetenskaper ->
Postens nummer:
Posten skapad:
2010-02-23 12:52
Posten ändrad:
2011-11-16 12:21

Visa i Endnote-format

Göteborgs universitet • Tel. 031-786 0000
© Göteborgs universitet 2007