Mutations to the formin homology 2 domain of INF2 protein have unexpected effects on actin polymerization and severing

Journal of Biological Chemistry

Volumn 287, Issue 41, 2012, Pages 34234-34245

  Ramabhadran, Vinay ^a   Gurel, Pinar S ^a   Higgs, Henry N ^a  

^a DARTMOUTH MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN FILAMENT; ACTIN POLYMERIZATION; BIOCHEMICAL CHARACTERISTICS; C-TERMINAL REGIONS; CAPPING PROTEINS; ENDOPLASMIC RETICULUM; EQUIVALENT EFFECT; FOCAL AND SEGMENTAL GLOMERULOSCLEROSIS; FORMIN HOMOLOGY 2; FORMINS; HUMAN DISEASE; INHIBITORY EFFECT; POLYMERIZATION ACTIVITY; SECRETORY PATHWAYS; TOTAL INTERNAL REFLECTIONS; UNIQUE FEATURES; WILD TYPES;

CELL MEMBRANES; CYTOLOGY; ELONGATION; POLYMERIZATION; REFRACTIVE INDEX;

PROTEINS;

ACTIN; FORMIN HOMOLOGY 2 DOMAIN PROTEIN; ISOLEUCINE; LYSINE; PROTEIN; PROTEIN INF2; PYRENE; UNCLASSIFIED DRUG;

ACTIN CAPPING; ACTIN FILAMENT; ACTIN POLYMERIZATION; ARTICLE; BIOLOGICAL ACTIVITY; CELL ELONGATION; CONTROLLED STUDY; DEPOLYMERIZATION; ENDOPLASMIC RETICULUM; HUMAN; MICROSCOPY; NONHUMAN; NUCLEOTIDE SEQUENCE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN METABOLISM; PROTEIN MODIFICATION; PROTEIN SEVERING; TOTAL INTERNAL REFLECTION MICROSCOPY;

ACTIN CAPPING PROTEINS; ACTIN CYTOSKELETON; ACTINS; AMINO ACID SUBSTITUTION; CELL LINE, TUMOR; CHARCOT-MARIE-TOOTH DISEASE; ENDOPLASMIC RETICULUM; GLOMERULOSCLEROSIS, FOCAL SEGMENTAL; HUMANS; MICROFILAMENT PROTEINS; MUTATION, MISSENSE; PROTEIN STRUCTURE, TERTIARY;

EID: 84867251545     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.365122     Document Type: Article

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