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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003886naa a2200517 4500
001oai:DiVA.org:umu-188651
003SwePub
008211018s2012 | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-1886512 URI
0247 a https://doi.org/10.1128/mcb.00713-122 DOI
040 a (SwePub)umu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Björkblom, Bennyu Turku Centre for Biotechnology, Åbo Akademi and University of Turku, BioCity, Turku, Finland4 aut0 (Swepub:umu)bebj0009
2451 0a c-Jun N-Terminal Kinase Phosphorylation of MARCKSL1 Determines Actin Stability and Migration in Neurons and in Cancer Cells
264 c 2023-03-20
264 1b American Society for Microbiology,c 2012
338 a print2 rdacarrier
520 a Cell migration is a fundamental biological function, critical during development and regeneration, whereas deregulated migration underlies neurological birth defects and cancer metastasis. MARCKS-like protein 1 (MARCKSL1) is widely expressed in nervous tissue, where, like Jun N-terminal protein kinase (JNK), it is required for neural tube formation, though the mechanism is unknown. Here we show that MARCKSL1 is directly phosphorylated by JNK on C-terminal residues (S120, T148, and T183). This phosphorylation enables MARCKSL1 to bundle and stabilize F-actin, increase filopodium numbers and dynamics, and retard migration in neurons. Conversely, when MARCKSL1 phosphorylation is inhibited, actin mobility increases and filopodium formation is compromised whereas lamellipodium formation is enhanced, as is cell migration. We find that MARCKSL1 mRNA is upregulated in a broad range of cancer types and that MARCKSL1 protein is strongly induced in primary prostate carcinomas. Gene knockdown in prostate cancer cells or in neurons reveals a critical role for MARCKSL1 in migration that is dependent on the phosphorylation state; phosphomimetic MARCKSL1 (MARCKSL1S120D,T148D,T183D) inhibits whereas dephospho-MARCKSL1S120A,T148A,T183A induces migration. In summary, these data show that JNK phosphorylation of MARCKSL1 regulates actin homeostasis, filopodium and lamellipodium formation, and neuronal migration under physiological conditions and that, when ectopically expressed in prostate cancer cells, MARCKSL1 again determines cell movement.
650 7a MEDICIN OCH HÄLSOVETENSKAPx Klinisk medicinx Cancer och onkologi0 (SwePub)302032 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Clinical Medicinex Cancer and Oncology0 (SwePub)302032 hsv//eng
650 7a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Cell- och molekylärbiologi0 (SwePub)301082 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Cell and Molecular Biology0 (SwePub)301082 hsv//eng
653 a Cell Biology
653 a Molecular Biology
7001 a Padzik, A.4 aut
7001 a Mohammad, H.4 aut
7001 a Westerlund, N.4 aut
7001 a Komulainen, E.4 aut
7001 a Hollos, P.4 aut
7001 a Parviainen, L.4 aut
7001 a Papageorgiou, A. C.4 aut
7001 a Iljin, K.4 aut
7001 a Kallioniemi, O.4 aut
7001 a Kallajoki, M.4 aut
7001 a Courtney, M. J.4 aut
7001 a Mågård, M.4 aut
7001 a James, P.4 aut
7001 a Coffey, E. T.4 aut
7102 a Turku Centre for Biotechnology, Åbo Akademi and University of Turku, BioCity, Turku, Finland4 org
7730 t Molecular and Cellular Biologyd : American Society for Microbiologyg 32:17, s. 3513-3526q 32:17<3513-3526x 0270-7306x 1098-5549
8564 u https://mcb.asm.org/content/mcb/32/17/3513.full.pdf
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-188651
8564 8u https://doi.org/10.1128/mcb.00713-12

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