Fascin Introduction: Difference between revisions

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Fascins bundle actin filaments into large, tightly packed hexagonal arrays that support diverse cellular processes including microvillar projections and filopodial extensions at the leading edge of migratory cells and that has been implicated in cell motility in several cell types (Jawhari et al 2003). Fascin should contain two actin binding domains since the protein cross-links actin filaments as a monomer (Cant & Cooley 1995). Fascin is widely expressed including the brain, blood, colon, lung, breast, ovary, and testis. In the brain, fascin expression has been localized to neurons, glial cells, and endothelial cells.(Nagai et al. 2008)  
Fascins bundle actin filaments into large, tightly packed hexagonal arrays that support diverse cellular processes including microvillar projections and filopodial extensions at the leading edge of migratory cells and that has been implicated in cell motility in several cell types (Jawhari et al 2003). Fascin should contain two actin binding domains since the protein cross-links actin filaments as a monomer (Cant & Cooley 1995). Fascin is widely expressed including the brain, blood, colon, lung, breast, ovary, and testis. In the brain, fascin expression has been localized to neurons, glial cells, and endothelial cells.(Nagai et al. 2008)  


One actin binding site is contained within the C-terminal half of fascin. This 21 amino acid region is a highly conserved domain is hydrophobic (Cant & Cooley 1995).   
Sequence alignment indicates that the members of the fascin family form a distinct class of proteins as they share a high degree of sequence identity with one another, but do not have significant sequence similarities with other known proteins (Tseng et al 2001).One actin binding site is contained within the C-terminal half of fascin. This 21 amino acid region is a highly conserved domain is hydrophobic (Cant & Cooley 1995).   




[[Fascin Abstract | Abstract]] | [[Fascin Introduction | Introduction]] | [[Fascin Methods | Methods]] | [[Fascin Results | Results]] | [[Fascin Discussion | Discussion]] | [[Fascin Conclusion | Conclusion]] | [[Fascin Appendix | Appendix]] | [[Fascin References | References]]
[[Fascin Abstract | Abstract]] | [[Fascin Introduction | Introduction]] | [[Fascin Methods | Methods]] | [[Fascin Results | Results]] | [[Fascin Discussion | Discussion]] | [[Fascin Conclusion | Conclusion]] | [[Fascin Appendix | Appendix]] | [[Fascin References | References]]
<br>[[Fascin 1 | Back to main page]]
<br>[[Fascin 1 | Back to main page]]

Revision as of 23:01, 15 June 2009

Intro

Actin bundles are necessary for the formation of specialized cellular processes, intercellular communication, and cell migration. Actin binding proteins guide the reorganization of the cytoskeleton that underlie these processes.

Fascins bundle actin filaments into large, tightly packed hexagonal arrays that support diverse cellular processes including microvillar projections and filopodial extensions at the leading edge of migratory cells and that has been implicated in cell motility in several cell types (Jawhari et al 2003). Fascin should contain two actin binding domains since the protein cross-links actin filaments as a monomer (Cant & Cooley 1995). Fascin is widely expressed including the brain, blood, colon, lung, breast, ovary, and testis. In the brain, fascin expression has been localized to neurons, glial cells, and endothelial cells.(Nagai et al. 2008)

Sequence alignment indicates that the members of the fascin family form a distinct class of proteins as they share a high degree of sequence identity with one another, but do not have significant sequence similarities with other known proteins (Tseng et al 2001).One actin binding site is contained within the C-terminal half of fascin. This 21 amino acid region is a highly conserved domain is hydrophobic (Cant & Cooley 1995).


Abstract | Introduction | Methods | Results | Discussion | Conclusion | Appendix | References
Back to main page