Prolactin augments progesterone-dependent expression of a nuclear P-type ATPase that associates with the RING domain of RUSH transcription factors in the endometrium.
Mansharamani
M
M
Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, 3601 4th Street, Lubbock, TX 79430, USA.
Chilton
B S
BS
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D002467:Cell Nucleus / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004717:Endometrium / Q000378:metabolism*; D005260:Female; D005786:Gene Expression Regulation; D006801:Humans; D063150:Polycomb Repressive Complex 1; D011374:Progesterone / Q000378:metabolism*; D011388:Prolactin / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D014157:Transcription Factors; D016335:Zinc Fingers / Q000502:physiology*
D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D012333:RNA, Messenger; C104270:SMARCA3 protein, Oryctolagus cuniculus; D014157:Transcription Factors; D011374:Progesterone; D011388:Prolactin; D063150:Polycomb Repressive Complex 1; C080355:RING1 protein, human; D000251:Adenosine Triphosphatases; C420204:RING-finger binding protein, Oryctolagus cuniculus; C030704:magnesium sodium potassium ATPase; D000254:Sodium-Potassium-Exchanging ATPase