Abstract
Myristoylated alanine-rich C kinase substrate (MARCKS) is an actin-binding, membrane-associated protein expressed during Xenopus embryogenesis. We analyzed its function in cytoskeletal regulation during gastrulation. Here, we show that blockade of its function impaired morphogenetic movements, including convergent extension. MARCKS was required for control of cell morphology, motility, adhesion, protrusive activity, and cortical actin formation in embryonic cells. We also demonstrate that the noncanonical Wnt pathway promotes the formation of lamellipodia- and filopodia-like protrusions and that MARCKS is necessary for this activity. These findings show that MARCKS regulates the cortical actin formation that is requisite for dynamic morphogenetic movements.
MeSH Terms
Actins/physiology
Animals
Cell Movement/physiology
Cloning, Molecular
Embryo, Nonmammalian/physiology
Gastrula/physiology
In Situ Hybridization
Intracellular Signaling Peptides and Proteins
Lipoproteins/genetics,physiology
Membrane Proteins/genetics,physiology
Myristoylated Alanine-Rich C Kinase Substrate
Protein Kinase C/physiology
RNA, Messenger/genetics
Reverse Transcriptase Polymerase Chain Reaction
Xenopus/embryology
Chemicals
Actins
Intracellular Signaling Peptides and Proteins
Lipoproteins
Membrane Proteins
RNA, Messenger
Myristoylated Alanine-Rich C Kinase Substrate
Protein Kinase C
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Iioka Hidekazu
Dept. of Developmental Biology, National Institute for Basic Biology, 38 Nishigonaka, Myodaiji Okazaki, Aichi 444-8585, Japan.
Ueno Naoto
Kinoshita Noriyuki
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