Ponticulin plays a role in the positional stabilization of pseudopods
Authors
Shutt, D. C.Wessels, D.
Wagenknecht, K.
Chandrasekhar, A.
Hitt, Anne L.
Luna, Elizabeth J.
Soll, D. R.
UMass Chan Affiliations
Department of Cell BiologyDocument Type
Journal ArticlePublication Date
1995-12-01Keywords
ActinsAnimals
Carrier Proteins
Cell Movement
Cell Size
Chemotaxis
Dictyostelium
Microfilament Proteins
Mutation
Pseudopodia
Cell Biology
Life Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
Ponticulin is a 17-kD glycoprotein that represents a major high affinity link between the plasma membrane and the cortical actin network of Dictyostelium. To assess the role of ponticulin in pseudopod extension and retraction, the motile behavior of two independently generated mutants lacking ponticulin was analyzed using computer-assisted two- and three-dimensional motion analysis systems. More than half of the lateral pseudopods formed off the substratum by ponticulin-minus cells slipped relative to the substratum during extension and retraction. In contrast, all pseudopods formed off the substratum by wild-type cells were positionally fixed in relation to the substratum. Ponticulin-minus cells also formed a greater proportion of both anterior and lateral pseudopods off the substratum and absorbed a greater proportion of lateral pseudopods into the uropod than wild-type cells. In a spatial gradient of cAMP, ponticulin-minus cells were less efficient in tracking the source of chemoattractant. Since ponticulin-minus cells extend and retract pseudopods with the same time course as wild-type cells, these behavioral defects in ponticulin-minus cells appear to be the consequence of pseudopod slippage. These results demonstrate that pseudopods formed off the substratum by wild-type cells are positionally fixed in relation to the substratum, that ponticulin is required for positional stabilization, and that the loss of ponticulin and the concomitant loss of positional stability of pseudopods correlate with a decrease in the efficiency of chemotaxis.Source
J Cell Biol. 1995 Dec;131(6 Pt 1):1495-506. Link to article on publisher's website
DOI
10.1083/jcb.131.6.1495Permanent Link to this Item
http://hdl.handle.net/20.500.14038/50768PubMed ID
8522606Related Resources
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Publisher PDF posted as allowed by the publisher's terms of use policy at: http://www.rupress.org/terms After the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Article under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode, or updates thereof.Distribution License
http://creativecommons.org/licenses/by-nc-sa/4.0/ae974a485f413a2113503eed53cd6c53
10.1083/jcb.131.6.1495
Scopus Count
Except where otherwise noted, this item's license is described as Publisher PDF posted as allowed by the publisher's terms of use policy at: http://www.rupress.org/terms After the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Article under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode, or updates thereof.