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The interaction between L1-type proteins and ankyrins - a master switch for L1-type CAM function
L1-type cell adhesion molecules (CAMs) are important mediators of neural differentiation, including axonal outgrowth and pathfinding and also of synapse formation and maintenance. In addition, their interactions with cytoskeletal components are highly conserved and regulated. How these different asp...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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SP Versita
2008
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2615246/ https://www.ncbi.nlm.nih.gov/pubmed/18839070 http://dx.doi.org/10.2478/s11658-008-0035-4 |
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author | Hortsch, Michael Nagaraj, Kakanahalli Godenschwege, Tanja A. |
author_facet | Hortsch, Michael Nagaraj, Kakanahalli Godenschwege, Tanja A. |
author_sort | Hortsch, Michael |
collection | PubMed |
description | L1-type cell adhesion molecules (CAMs) are important mediators of neural differentiation, including axonal outgrowth and pathfinding and also of synapse formation and maintenance. In addition, their interactions with cytoskeletal components are highly conserved and regulated. How these different aspects of CAM functionality relate to each other is not well understood. Based on results from our and other laboratories we propose that ankyrin-binding to L1-type CAMs provides a master switch. The interaction with ankyrins directs L1-type adhesive proteins into different functional contexts, either ankyrin-independent functions, such as neurite outgrowth and axonal pathfinding or into ankyrin-dependent functions, such as L1’s role at axon initial segments (AIS), paranodal regions, synapses and in dendrites. |
format | Text |
id | pubmed-2615246 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | SP Versita |
record_format | MEDLINE/PubMed |
spelling | pubmed-26152462010-01-01 The interaction between L1-type proteins and ankyrins - a master switch for L1-type CAM function Hortsch, Michael Nagaraj, Kakanahalli Godenschwege, Tanja A. Cell Mol Biol Lett Mini Review L1-type cell adhesion molecules (CAMs) are important mediators of neural differentiation, including axonal outgrowth and pathfinding and also of synapse formation and maintenance. In addition, their interactions with cytoskeletal components are highly conserved and regulated. How these different aspects of CAM functionality relate to each other is not well understood. Based on results from our and other laboratories we propose that ankyrin-binding to L1-type CAMs provides a master switch. The interaction with ankyrins directs L1-type adhesive proteins into different functional contexts, either ankyrin-independent functions, such as neurite outgrowth and axonal pathfinding or into ankyrin-dependent functions, such as L1’s role at axon initial segments (AIS), paranodal regions, synapses and in dendrites. SP Versita 2008-10-06 /pmc/articles/PMC2615246/ /pubmed/18839070 http://dx.doi.org/10.2478/s11658-008-0035-4 Text en © © Versita Warsaw and Springer-Verlag Berlin Heidelberg 2008 |
spellingShingle | Mini Review Hortsch, Michael Nagaraj, Kakanahalli Godenschwege, Tanja A. The interaction between L1-type proteins and ankyrins - a master switch for L1-type CAM function |
title | The interaction between L1-type proteins and ankyrins - a master switch for L1-type CAM function |
title_full | The interaction between L1-type proteins and ankyrins - a master switch for L1-type CAM function |
title_fullStr | The interaction between L1-type proteins and ankyrins - a master switch for L1-type CAM function |
title_full_unstemmed | The interaction between L1-type proteins and ankyrins - a master switch for L1-type CAM function |
title_short | The interaction between L1-type proteins and ankyrins - a master switch for L1-type CAM function |
title_sort | interaction between l1-type proteins and ankyrins - a master switch for l1-type cam function |
topic | Mini Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2615246/ https://www.ncbi.nlm.nih.gov/pubmed/18839070 http://dx.doi.org/10.2478/s11658-008-0035-4 |
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