Nance-Horan Syndrome-like 1 protein negatively regulates Scar/WAVE-Arp2/3 activity and inhibits lamellipodia stability and cell migration

Standard

Nance-Horan Syndrome-like 1 protein negatively regulates Scar/WAVE-Arp2/3 activity and inhibits lamellipodia stability and cell migration. / Law, Ah-Lai; Jalal, Shamsinar; Pallett, Tommy; Mosis, Fuad; Guni, Ahmad; Brayford, Simon; Yolland, Lawrence; Marcotti, Stefania; Levitt, James A; Poland, Simon P; Rowe-Sampson, Maia; Jandke, Anett; Köchl, Robert; Pula, Giordano; Ameer-Beg, Simon M; Stramer, Brian Marc; Krause, Matthias.

in: NAT COMMUN, Jahrgang 12, Nr. 1, 28.09.2021, S. 5687.

Publikationen: SCORING: Beitrag in Fachzeitschrift/ZeitungSCORING: ZeitschriftenaufsatzForschungBegutachtung

Harvard

Law, A-L, Jalal, S, Pallett, T, Mosis, F, Guni, A, Brayford, S, Yolland, L, Marcotti, S, Levitt, JA, Poland, SP, Rowe-Sampson, M, Jandke, A, Köchl, R, Pula, G, Ameer-Beg, SM, Stramer, BM & Krause, M 2021, 'Nance-Horan Syndrome-like 1 protein negatively regulates Scar/WAVE-Arp2/3 activity and inhibits lamellipodia stability and cell migration', NAT COMMUN, Jg. 12, Nr. 1, S. 5687. https://doi.org/10.1038/s41467-021-25916-6

APA

Law, A-L., Jalal, S., Pallett, T., Mosis, F., Guni, A., Brayford, S., Yolland, L., Marcotti, S., Levitt, J. A., Poland, S. P., Rowe-Sampson, M., Jandke, A., Köchl, R., Pula, G., Ameer-Beg, S. M., Stramer, B. M., & Krause, M. (2021). Nance-Horan Syndrome-like 1 protein negatively regulates Scar/WAVE-Arp2/3 activity and inhibits lamellipodia stability and cell migration. NAT COMMUN, 12(1), 5687. https://doi.org/10.1038/s41467-021-25916-6

Vancouver

Bibtex

@article{5f5b310caed4436fac1244e539596c56,
title = "Nance-Horan Syndrome-like 1 protein negatively regulates Scar/WAVE-Arp2/3 activity and inhibits lamellipodia stability and cell migration",
abstract = "Cell migration is important for development and its aberrant regulation contributes to many diseases. The Scar/WAVE complex is essential for Arp2/3 mediated lamellipodia formation during mesenchymal cell migration and several coinciding signals activate it. However, so far, no direct negative regulators are known. Here we identify Nance-Horan Syndrome-like 1 protein (NHSL1) as a direct binding partner of the Scar/WAVE complex, which co-localise at protruding lamellipodia. This interaction is mediated by the Abi SH3 domain and two binding sites in NHSL1. Furthermore, active Rac binds to NHSL1 at two regions that mediate leading edge targeting of NHSL1. Surprisingly, NHSL1 inhibits cell migration through its interaction with the Scar/WAVE complex. Mechanistically, NHSL1 may reduce cell migration efficiency by impeding Arp2/3 activity, as measured in cells using a Arp2/3 FRET-FLIM biosensor, resulting in reduced F-actin density of lamellipodia, and consequently impairing the stability of lamellipodia protrusions.",
author = "Ah-Lai Law and Shamsinar Jalal and Tommy Pallett and Fuad Mosis and Ahmad Guni and Simon Brayford and Lawrence Yolland and Stefania Marcotti and Levitt, {James A} and Poland, {Simon P} and Maia Rowe-Sampson and Anett Jandke and Robert K{\"o}chl and Giordano Pula and Ameer-Beg, {Simon M} and Stramer, {Brian Marc} and Matthias Krause",
note = "{\textcopyright} 2021. The Author(s).",
year = "2021",
month = sep,
day = "28",
doi = "10.1038/s41467-021-25916-6",
language = "English",
volume = "12",
pages = "5687",
journal = "NAT COMMUN",
issn = "2041-1723",
publisher = "NATURE PUBLISHING GROUP",
number = "1",

}

RIS

TY - JOUR

T1 - Nance-Horan Syndrome-like 1 protein negatively regulates Scar/WAVE-Arp2/3 activity and inhibits lamellipodia stability and cell migration

AU - Law, Ah-Lai

AU - Jalal, Shamsinar

AU - Pallett, Tommy

AU - Mosis, Fuad

AU - Guni, Ahmad

AU - Brayford, Simon

AU - Yolland, Lawrence

AU - Marcotti, Stefania

AU - Levitt, James A

AU - Poland, Simon P

AU - Rowe-Sampson, Maia

AU - Jandke, Anett

AU - Köchl, Robert

AU - Pula, Giordano

AU - Ameer-Beg, Simon M

AU - Stramer, Brian Marc

AU - Krause, Matthias

N1 - © 2021. The Author(s).

PY - 2021/9/28

Y1 - 2021/9/28

N2 - Cell migration is important for development and its aberrant regulation contributes to many diseases. The Scar/WAVE complex is essential for Arp2/3 mediated lamellipodia formation during mesenchymal cell migration and several coinciding signals activate it. However, so far, no direct negative regulators are known. Here we identify Nance-Horan Syndrome-like 1 protein (NHSL1) as a direct binding partner of the Scar/WAVE complex, which co-localise at protruding lamellipodia. This interaction is mediated by the Abi SH3 domain and two binding sites in NHSL1. Furthermore, active Rac binds to NHSL1 at two regions that mediate leading edge targeting of NHSL1. Surprisingly, NHSL1 inhibits cell migration through its interaction with the Scar/WAVE complex. Mechanistically, NHSL1 may reduce cell migration efficiency by impeding Arp2/3 activity, as measured in cells using a Arp2/3 FRET-FLIM biosensor, resulting in reduced F-actin density of lamellipodia, and consequently impairing the stability of lamellipodia protrusions.

AB - Cell migration is important for development and its aberrant regulation contributes to many diseases. The Scar/WAVE complex is essential for Arp2/3 mediated lamellipodia formation during mesenchymal cell migration and several coinciding signals activate it. However, so far, no direct negative regulators are known. Here we identify Nance-Horan Syndrome-like 1 protein (NHSL1) as a direct binding partner of the Scar/WAVE complex, which co-localise at protruding lamellipodia. This interaction is mediated by the Abi SH3 domain and two binding sites in NHSL1. Furthermore, active Rac binds to NHSL1 at two regions that mediate leading edge targeting of NHSL1. Surprisingly, NHSL1 inhibits cell migration through its interaction with the Scar/WAVE complex. Mechanistically, NHSL1 may reduce cell migration efficiency by impeding Arp2/3 activity, as measured in cells using a Arp2/3 FRET-FLIM biosensor, resulting in reduced F-actin density of lamellipodia, and consequently impairing the stability of lamellipodia protrusions.

U2 - 10.1038/s41467-021-25916-6

DO - 10.1038/s41467-021-25916-6

M3 - SCORING: Journal article

C2 - 34584076

VL - 12

SP - 5687

JO - NAT COMMUN

JF - NAT COMMUN

SN - 2041-1723

IS - 1

ER -