PMID- 10066790
OWN - NLM
STAT- MEDLINE
DCOM- 19990413
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 11
DP  - 1999 Mar 12
TI  - AP-4, a novel protein complex related to clathrin adaptors.
PG  - 7278-85
AB  - Here we report the identification and characterization of AP-4, a novel protein
      complex related to the heterotetrameric AP-1, AP-2, and AP-3 adaptors that
      mediate protein sorting in the endocytic and late secretory pathways. The key to 
      the identification of this complex was the cloning and sequencing of two widely
      expressed, mammalian cDNAs encoding new homologs of the adaptor beta and sigma
      subunits named beta4 and sigma4, respectively. An antibody to beta4 recognized in
      human cells an approximately 83-kDa polypeptide that exists in both soluble and
      membrane-associated forms. Gel filtration, sedimentation velocity, and
      immunoprecipitation experiments revealed that beta4 is a component of a
      multisubunit complex (AP-4) that also contains the sigma4 polypeptide and two
      additional adaptor subunit homologs named mu4 (mu-ARP2) and epsilon.
      Immunofluorescence analyses showed that AP-4 is associated with the trans-Golgi
      network or an adjacent structure and that this association is sensitive to the
      drug brefeldin A. We propose that, like the related AP-1, AP-2, and AP-3
      complexes, AP-4 plays a role in signal-mediated trafficking of integral membrane 
      proteins in mammalian cells.
FAU - Dell'Angelica, E C
AU  - Dell'Angelica EC
AD  - Cell Biology and Metabolism Branch, NICHD, National Institutes of Health,
      Bethesda, Maryland 20892, USA.
FAU - Mullins, C
AU  - Mullins C
FAU - Bonifacino, J S
AU  - Bonifacino JS
LA  - eng
SI  - GENBANK/AF092093
SI  - GENBANK/AF092094
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Adaptor Protein Complex alpha Subunits)
RN  - 0 (Adaptor Proteins, Vesicular Transport)
RN  - 0 (Clathrin)
RN  - 0 (DNA, Complementary)
RN  - 0 (Membrane Proteins)
RN  - 0 (Monomeric Clathrin Assembly Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (clathrin assembly protein AP180)
SB  - IM
MH  - Adaptor Protein Complex alpha Subunits
MH  - Adaptor Proteins, Vesicular Transport
MH  - Amino Acid Sequence
MH  - Animals
MH  - Clathrin/*chemistry
MH  - DNA, Complementary
MH  - HeLa Cells
MH  - Humans
MH  - Membrane Proteins/*chemistry
MH  - Mice
MH  - Microscopy, Fluorescence
MH  - Molecular Sequence Data
MH  - *Monomeric Clathrin Assembly Proteins
MH  - Nerve Tissue Proteins/*chemistry/genetics/metabolism
MH  - Phosphoproteins/*chemistry/genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Subcellular Fractions/chemistry
EDAT- 1999/03/06 00:00
MHDA- 1999/03/06 00:01
CRDT- 1999/03/06 00:00
PHST- 1999/03/06 00:00 [pubmed]
PHST- 1999/03/06 00:01 [medline]
PHST- 1999/03/06 00:00 [entrez]
AID - 10.1074/jbc.274.11.7278 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Mar 12;274(11):7278-85. doi: 10.1074/jbc.274.11.7278.