LIMK1 activity regulates Rab5 endosome trafficking

The endosomal recycling pathway involves the regulated balance of two processes; recycling endocytosed proteins to the cell membrane and targeting such proteins for lysosomal degradation. The recycling pathway alters the composition of plasma membrane proteins such as cell-adhesion molecules (CAMs)....

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Main Author: Lee, Bernadette Jia Rong
Other Authors: Koh Cheng Gee
Format: Final Year Project
Language:English
Published: 2018
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Online Access:http://hdl.handle.net/10356/74199
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-741992023-02-28T18:07:32Z LIMK1 activity regulates Rab5 endosome trafficking Lee, Bernadette Jia Rong Koh Cheng Gee School of Biological Sciences DRNTU::Science The endosomal recycling pathway involves the regulated balance of two processes; recycling endocytosed proteins to the cell membrane and targeting such proteins for lysosomal degradation. The recycling pathway alters the composition of plasma membrane proteins such as cell-adhesion molecules (CAMs). While cadherin endocytosis is essential for developmental processes, its deregulation has been known to contribute to cancer metastasis. Motor proteins are required for endocytic trafficking by tethering to membranes and moving them along cytoskeletal filaments, thus providing the force required for membrane deformation and scission which is responsible for promoting endosomal sorting and the formation of transport intermediates. LIM domain kinase 1 (LIMK1) has been extensively described to regulate actin dynamics by phosphorylating cofilin. However, its role on microtubule cytoskeleton remains to be elucidated. Hence, investigation is done on the role of LIMK1 activity on dynein and endocytic recycling in this study. As an initial step to elucidate the role of LIMK1 on dynein, GST pull-down and co-immunoprecipitation is performed to demonstrate LIMK1 association with dynein. In addition, live cell imaging of HeLa cells over-expressing constitutively active LIMK1-T508EE displayed a marked retardation in the trafficking speed of Rab5 particles, which are present on early endosomes. Internalisation of N-cadherin was also perturbed in LIMK1-T508EE overexpressing cells. Bachelor of Science in Biological Sciences 2018-05-08T01:02:55Z 2018-05-08T01:02:55Z 2018 Final Year Project (FYP) http://hdl.handle.net/10356/74199 en Nanyang Technological University 23 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Science
spellingShingle DRNTU::Science
Lee, Bernadette Jia Rong
LIMK1 activity regulates Rab5 endosome trafficking
description The endosomal recycling pathway involves the regulated balance of two processes; recycling endocytosed proteins to the cell membrane and targeting such proteins for lysosomal degradation. The recycling pathway alters the composition of plasma membrane proteins such as cell-adhesion molecules (CAMs). While cadherin endocytosis is essential for developmental processes, its deregulation has been known to contribute to cancer metastasis. Motor proteins are required for endocytic trafficking by tethering to membranes and moving them along cytoskeletal filaments, thus providing the force required for membrane deformation and scission which is responsible for promoting endosomal sorting and the formation of transport intermediates. LIM domain kinase 1 (LIMK1) has been extensively described to regulate actin dynamics by phosphorylating cofilin. However, its role on microtubule cytoskeleton remains to be elucidated. Hence, investigation is done on the role of LIMK1 activity on dynein and endocytic recycling in this study. As an initial step to elucidate the role of LIMK1 on dynein, GST pull-down and co-immunoprecipitation is performed to demonstrate LIMK1 association with dynein. In addition, live cell imaging of HeLa cells over-expressing constitutively active LIMK1-T508EE displayed a marked retardation in the trafficking speed of Rab5 particles, which are present on early endosomes. Internalisation of N-cadherin was also perturbed in LIMK1-T508EE overexpressing cells.
author2 Koh Cheng Gee
author_facet Koh Cheng Gee
Lee, Bernadette Jia Rong
format Final Year Project
author Lee, Bernadette Jia Rong
author_sort Lee, Bernadette Jia Rong
title LIMK1 activity regulates Rab5 endosome trafficking
title_short LIMK1 activity regulates Rab5 endosome trafficking
title_full LIMK1 activity regulates Rab5 endosome trafficking
title_fullStr LIMK1 activity regulates Rab5 endosome trafficking
title_full_unstemmed LIMK1 activity regulates Rab5 endosome trafficking
title_sort limk1 activity regulates rab5 endosome trafficking
publishDate 2018
url http://hdl.handle.net/10356/74199
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