Cell migration and invadopodia formation require a membrane-binding domain of CARMIL2

Journal of Biological Chemistry

Volumn 291, Issue 3, 2016, Pages 1076-1091

  Lanier, M Hunter ^a   McConnell, Patrick ^a   Cooper, John A ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINS; CELLS; CYTOLOGY; MEMBRANES;

ACTIN-BASED CELLS; CAPPING PROTEINS; CRITICAL DETERMINANT; HYDROPHOBIC RESIDUES; INTERMEDIATE FILAMENTS; MEMBRANE LOCALIZATION; MULTIDOMAIN PROTEINS; SEQUENCE ANALYSIS;

PROTEINS;

CELL PROTEIN; PROTEIN CARMIL2; PROTEIN CARMIL3; UNCLASSIFIED DRUG; VIMENTIN; ACTIN BINDING PROTEIN; CD2-ASSOCIATED PROTEIN; CYTOSKELETON PROTEIN; HYBRID PROTEIN; ISOPROTEIN; LIPOSOME; LRRC16A PROTEIN, HUMAN; PEPTIDE FRAGMENT; PHOTOPROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

ARTICLE; CELL MIGRATION; CELL POLARITY; CONTROLLED STUDY; DEGRADATION KINETICS; HUMAN; HUMAN CELL; HYDROPHOBICITY; INTERMEDIATE FILAMENT; MEMBRANE BINDING; NONHUMAN; PINOCYTOSIS; PODOSOME; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PURIFICATION; RESIDUE ANALYSIS; AMINO ACID SEQUENCE; ANTAGONISTS AND INHIBITORS; CELL LINE; CELL MEMBRANE; CELL MOTION; CHEMICAL PHENOMENA; CHEMISTRY; COMPARATIVE STUDY; CONSERVED SEQUENCE; GENETICS; METABOLISM; MUTATION; PROTEIN DATABASE; PROTEIN TRANSPORT; RNA INTERFERENCE;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; CELL LINE; CELL MEMBRANE; CELL MOVEMENT; CONSERVED SEQUENCE; CYTOSKELETAL PROTEINS; DATABASES, PROTEIN; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; INTERMEDIATE FILAMENTS; LIPOSOMES; LUMINESCENT PROTEINS; MICROFILAMENT PROTEINS; MUTATION; PEPTIDE FRAGMENTS; PODOSOMES; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN ISOFORMS; PROTEIN TRANSPORT; RECOMBINANT FUSION PROTEINS; RNA INTERFERENCE; VIMENTIN;

EID: 84954532821     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.676882     Document Type: Article

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