Myosin 1G is an abundant class I myosin in lymphocytes whose localization at the plasma membrane depends on its ancient divergent pleckstrin homology (PH) domain (Myo1PH)

Journal of Biological Chemistry

Volumn 285, Issue 12, 2010, Pages 8675-8686

  Patino Lopez, Genaro ^a   Aravind, L ^b   Dong, Xiaoyun ^a   Kruhlak, Michael J ^a   Ostap, E Michael ^c   Shaw, Stephen ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SPECIFICITIES; BISPHOSPHATES; CLASS I; EUKARYOTIC PROTEINS; F-ACTIN; ISOFORMS; LIPID BINDING SITES; LONG TAIL; MASS SPECTROMETRIC ANALYSIS; MEMBRANE ASSOCIATION; MEMBRANE LOCALIZATION; MOTOR DOMAIN; PHOSPHATIDYLINOSITOL; PHOSPHOINOSITIDES; PLASMA MEMBRANES; PLECKSTRIN HOMOLOGY DOMAINS; SEQUENCE ANALYSIS; T-LYMPHOCYTES;

BINDING ENERGY; CELL MEMBRANES; PELLETIZING; PROTEINS;

MEMBRANES;

F ACTIN; MYOSIN 1F; MYOSIN 1G; MYOSIN I; MYOSIN IIA; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PLECKSTRIN; UNCLASSIFIED DRUG; ISOPROTEIN; LIPID; MYOSIN; PHOSPHOPROTEIN; PLASMA PROTEIN; PLATELET PROTEIN P47;

ALPHA HELIX; ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; BINDING SITE; CELL MEMBRANE; CONTROLLED STUDY; ENZYME RELEASE; HUMAN; HUMAN CELL; LYMPHOCYTE; MASS SPECTROMETRY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN MOTIF; CHEMICAL MODEL; CHEMISTRY; FLUORESCENCE MICROSCOPY; LEUKEMIA CELL LINE; METABOLISM; METHODOLOGY; PHYSIOLOGY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; STATIC ELECTRICITY;

EUKARYOTA; PROKARYOTA;

BINDING SITES; BLOOD PROTEINS; CELL MEMBRANE; HUMANS; JURKAT CELLS; LIPIDS; LYMPHOCYTES; MASS SPECTROMETRY; MICROSCOPY, FLUORESCENCE; MODELS, CHEMICAL; MYOSIN TYPE I; MYOSINS; PHOSPHOPROTEINS; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; STATIC ELECTRICITY;

EID: 77950573946     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.086959     Document Type: Article

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