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Lincing Complex Functions At The Nuclear Envelope%3a What The Molecular Architecture Of The Linc Complex Can Reveal About Its Function. by Rothballer%2c Andrea
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1LINCing Complex Functions At The Nuclear Envelope: What The Molecular Architecture Of The LINC Complex Can Reveal About Its Function.
By Rothballer, Andrea, Schwartz, Thomas U. and Kutay, Ulrike
This article is from Nucleus , volume 4 . Abstract Linker of nucleoskeleton and cytoskeleton (LINC) complexes span the double membrane of the nuclear envelope (NE) and physically connect nuclear structures to cytoskeletal elements. LINC complexes are envisioned as force transducers in the NE, which facilitate processes like nuclear anchorage and migration, or chromosome movements. The complexes are built from members of two evolutionary conserved families of transmembrane (TM) proteins, the SUN (Sad1/UNC-84) domain proteins in the inner nuclear membrane (INM) and the KASH (Klarsicht/ANC-1/SYNE homology) domain proteins in the outer nuclear membrane (ONM). In the lumen of the NE, the SUN and KASH domains engage in an intimate assembly to jointly form a NE bridge. Detailed insights into the molecular architecture and atomic structure of LINC complexes have recently revealed the molecular basis of nucleo-cytoskeletal coupling. They bear important implications for LINC complex function and suggest new potential and as yet unexplored roles, which the complexes may play in the cell.
“LINCing Complex Functions At The Nuclear Envelope: What The Molecular Architecture Of The LINC Complex Can Reveal About Its Function.” Metadata:
- Title: ➤ LINCing Complex Functions At The Nuclear Envelope: What The Molecular Architecture Of The LINC Complex Can Reveal About Its Function.
- Authors: Rothballer, AndreaSchwartz, Thomas U.Kutay, Ulrike
- Language: English
Edition Identifiers:
- Internet Archive ID: pubmed-PMC3585024
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The book is available for download in "texts" format, the size of the file-s is: 8.51 Mbs, the file-s for this book were downloaded 76 times, the file-s went public at Tue Oct 28 2014.
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