PMID- 14532018
OWN - NLM
STAT- MEDLINE
DCOM- 20031202
LR  - 20200930
IS  - 0363-6143 (Print)
IS  - 0363-6143 (Linking)
VI  - 285
IP  - 5
DP  - 2003 Nov
TI  - Potential role for a novel AP180-related protein during endocytosis in MDCK 
      cells.
PG  - C995-1008
AB  - Clathrin assembly protein, AP180, was originally identified as a brain-specific 
      protein localized to the presynaptic junction. AP180 acts to limit vesicle size 
      and maintain a pool of releasable synaptic vesicles during rapid recycling. In 
      this study, we show that polarized epithelial Madin-Darby canine kidney (MDCK) 
      cells express two AP180-related proteins: the ubiquitously expressed 62-kDa 
      clathrin assembly lymphoid myeloid leukemia (CALM, AP180-2) protein and a novel 
      high-molecular-weight homolog that we have named AP180-3. Sequence analysis of 
      AP180-3 expressed in MDCK cells shows high homology to AP180 from rat brain. 
      AP180-3 contains conserved motifs found in brain-specific AP180, including the 
      epsin NH2-terminal homology (ENTH) domain, the binding site for the alpha-subunit 
      of AP-2, and DLL repeats. Our studies show that AP180-3 from MDCK cells forms 
      complexes with AP-2 and clathrin and that membrane recruitment of these complexes 
      is modulated by phosphorylation. We demonstrate by immunohistochemistry that 
      AP180-3 is localized to cytoplasmic vesicles in MDCK cells and is also present in 
      tubule epithelial cells from mouse kidney. We observed by immunodetection that a 
      high-molecular-weight AP180-related protein is expressed in numerous cells in 
      addition to MDCK cells.
FAU - Kusner, Linda
AU  - Kusner L
AD  - Dept. of Physiology and Biophysics, Case Western Reserve University School of 
      Medicine, 10900 Euclid Avenue, Cleveland, OH 44106-4970, USA.
FAU - Carlin, Cathleen
AU  - Carlin C
LA  - eng
GR  - P50 DK 54178/DK/NIDDK NIH HHS/United States
GR  - P50 DK 57306/DK/NIDDK NIH HHS/United States
GR  - T32 HL 07653/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Am J Physiol Cell Physiol
JT  - American journal of physiology. Cell physiology
JID - 100901225
RN  - 0 (Monomeric Clathrin Assembly Proteins)
RN  - 0 (Protein Isoforms)
RN  - 0 (clathrin assembly protein AP180)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Cell Line
MH  - Dogs
MH  - Endocytosis/*physiology
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Molecular Sequence Data
MH  - Monomeric Clathrin Assembly Proteins/analysis/genetics/*physiology
MH  - Protein Isoforms/genetics/physiology
MH  - Rats
MH  - Sequence Homology, Amino Acid
EDAT- 2003/10/09 05:00
MHDA- 2003/12/03 05:00
CRDT- 2003/10/09 05:00
PHST- 2003/10/09 05:00 [pubmed]
PHST- 2003/12/03 05:00 [medline]
PHST- 2003/10/09 05:00 [entrez]
AID - 285/5/C995 [pii]
AID - 10.1152/ajpcell.00079.2003 [doi]
PST - ppublish
SO  - Am J Physiol Cell Physiol. 2003 Nov;285(5):C995-1008. doi: 
      10.1152/ajpcell.00079.2003.