The RNA-binding protein LARP4 regulates cancer cell migration and invasion

Shailaja Seetharaman; Ella Flemyng; Jiazhen Shen; Maria R. Conte; Anne J. Ridley

doi:10.1002/cm.21336

The RNA-binding protein LARP4 regulates cancer cell migration and invasion

Shailaja Seetharaman, Ella Flemyng, Jiazhen Shen, Maria R. Conte, Anne J. Ridley^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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Abstract

LARP4 is a La-related RNA-binding protein implicated in regulating mRNA translation, which interacts with poly(A)-binding protein (PABP). We previously identified LARP4 in an RNAi screen as one of several genes that regulate the shape of PC3 prostate cancer cells. Here we show that LARP4 depletion induces cell elongation in PC3 cells and MDA-MB-231 breast cancer cells. LARP4 depletion increases cell migration and invasion, as well as inducing invasive cell protrusions in 3D Matrigel. Conversely, LARP4 over-expression reduces cell elongation and increases cell circularity. LARP4 mutations are found in a variety of cancers. Introduction of some of these cancer-associated mutations, including a truncation mutant, into LARP4 enhances its effects on cell morphology. The truncation mutant shows enhanced interaction with PABP. We propose that LARP4 inhibits migration and invasion of cancer cells, and that some cancer-associated mutations stimulate these effects of LARP4.

Original language	English
Journal	Cytoskeleton (Hoboken, N.J.)
DOIs	https://doi.org/10.1002/cm.21336
Publication status	Published - 26 Sept 2016

Keywords

Actin cytoskeleton
Cancer cells
Cell morphology
Immunofluorescence
La-related proteins

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1002/cm.21336Licence: CC BY

The RNA-binding protein_SHEN_Accepted 7Sept2016 GOLD VoRFinal published version, 622 KBLicence: CC BY

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title = "The RNA-binding protein LARP4 regulates cancer cell migration and invasion",

abstract = "LARP4 is a La-related RNA-binding protein implicated in regulating mRNA translation, which interacts with poly(A)-binding protein (PABP). We previously identified LARP4 in an RNAi screen as one of several genes that regulate the shape of PC3 prostate cancer cells. Here we show that LARP4 depletion induces cell elongation in PC3 cells and MDA-MB-231 breast cancer cells. LARP4 depletion increases cell migration and invasion, as well as inducing invasive cell protrusions in 3D Matrigel. Conversely, LARP4 over-expression reduces cell elongation and increases cell circularity. LARP4 mutations are found in a variety of cancers. Introduction of some of these cancer-associated mutations, including a truncation mutant, into LARP4 enhances its effects on cell morphology. The truncation mutant shows enhanced interaction with PABP. We propose that LARP4 inhibits migration and invasion of cancer cells, and that some cancer-associated mutations stimulate these effects of LARP4.",

keywords = "Actin cytoskeleton, Cancer cells, Cell morphology, Immunofluorescence, La-related proteins",

author = "Shailaja Seetharaman and Ella Flemyng and Jiazhen Shen and Conte, {Maria R.} and Ridley, {Anne J.}",

year = "2016",

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doi = "10.1002/cm.21336",

language = "English",

journal = "Cytoskeleton (Hoboken, N.J.)",

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T1 - The RNA-binding protein LARP4 regulates cancer cell migration and invasion

AU - Seetharaman, Shailaja

AU - Flemyng, Ella

AU - Shen, Jiazhen

AU - Conte, Maria R.

AU - Ridley, Anne J.

PY - 2016/9/26

Y1 - 2016/9/26

N2 - LARP4 is a La-related RNA-binding protein implicated in regulating mRNA translation, which interacts with poly(A)-binding protein (PABP). We previously identified LARP4 in an RNAi screen as one of several genes that regulate the shape of PC3 prostate cancer cells. Here we show that LARP4 depletion induces cell elongation in PC3 cells and MDA-MB-231 breast cancer cells. LARP4 depletion increases cell migration and invasion, as well as inducing invasive cell protrusions in 3D Matrigel. Conversely, LARP4 over-expression reduces cell elongation and increases cell circularity. LARP4 mutations are found in a variety of cancers. Introduction of some of these cancer-associated mutations, including a truncation mutant, into LARP4 enhances its effects on cell morphology. The truncation mutant shows enhanced interaction with PABP. We propose that LARP4 inhibits migration and invasion of cancer cells, and that some cancer-associated mutations stimulate these effects of LARP4.

AB - LARP4 is a La-related RNA-binding protein implicated in regulating mRNA translation, which interacts with poly(A)-binding protein (PABP). We previously identified LARP4 in an RNAi screen as one of several genes that regulate the shape of PC3 prostate cancer cells. Here we show that LARP4 depletion induces cell elongation in PC3 cells and MDA-MB-231 breast cancer cells. LARP4 depletion increases cell migration and invasion, as well as inducing invasive cell protrusions in 3D Matrigel. Conversely, LARP4 over-expression reduces cell elongation and increases cell circularity. LARP4 mutations are found in a variety of cancers. Introduction of some of these cancer-associated mutations, including a truncation mutant, into LARP4 enhances its effects on cell morphology. The truncation mutant shows enhanced interaction with PABP. We propose that LARP4 inhibits migration and invasion of cancer cells, and that some cancer-associated mutations stimulate these effects of LARP4.

KW - Actin cytoskeleton

KW - Cancer cells

KW - Cell morphology

KW - Immunofluorescence

KW - La-related proteins

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DO - 10.1002/cm.21336

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SN - 1949-3584

JO - Cytoskeleton (Hoboken, N.J.)

JF - Cytoskeleton (Hoboken, N.J.)

ER -

The RNA-binding protein LARP4 regulates cancer cell migration and invasion

Abstract

Keywords

UN SDGs

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