PMID- 10514494
OWN - NLM
STAT- MEDLINE
DCOM- 19991119
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 42
DP  - 1999 Oct 15
TI  - Direct interaction of the trans-Golgi network membrane protein, TGN38, with the
      F-actin binding protein, neurabin.
PG  - 30080-6
AB  - TGN38 is a type I integral membrane protein that constitutively cycles between
      the trans-Golgi network (TGN) and plasma membrane. The cytosolic domain of TGN38 
      interacts with AP2 clathrin adaptor complexes via the tyrosine-containing motif
      (-SDYQRL-) to direct internalization from the plasma membrane. This motif has
      previously been shown to direct both internalization and subsequent TGN targeting
      of TGN38. We have used the cytosolic domain of TGN38 in a two-hybrid screen, and 
      we have identified the brain-specific F-actin binding protein neurabin-I as a
      TGN38-binding protein. We demonstrate a direct interaction between TGN38 and the 
      ubiquitous homologue of neurabin-I, neurabin-II (also called spinophilin). We
      have used a combination of yeast two-hybrid and in vitro protein interaction
      assays to show that this interaction is dependent on the serine (but not
      tyrosine) residue of the known TGN38 trafficking motif. We show that TGN38
      interacts with the coiled coil region of neurabin in vitro and binds
      preferentially with the dimeric form of neurabin. TGN38 and neurabin also
      interact in vivo as demonstrated by coimmunoprecipitation from stably transfected
      PC12 cells. These data suggest that neurabin provides a direct physical link
      between TGN38-containing membranes and the actin cytoskeleton.
FAU - Stephens, D J
AU  - Stephens DJ
AD  - Department of Biochemistry, University of Bristol, School of Medical Sciences,
      University Walk, Bristol BS8 1TD, United Kingdom.
FAU - Banting, G
AU  - Banting G
LA  - eng
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 (Actins)
RN  - 0 (Glycoproteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Microfilament Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Protein Isoforms)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Tgoln2 protein, rat)
RN  - 0 (neurabin)
SB  - IM
MH  - Actins/*metabolism
MH  - Animals
MH  - *Glycoproteins
MH  - Golgi Apparatus/*metabolism
MH  - Membrane Glycoproteins/*metabolism
MH  - *Membrane Proteins
MH  - Microfilament Proteins/*metabolism
MH  - Nerve Tissue Proteins/*metabolism
MH  - PC12 Cells
MH  - Protein Binding
MH  - Protein Isoforms/metabolism
MH  - Rats
MH  - Recombinant Proteins/metabolism
EDAT- 1999/10/09 00:00
MHDA- 1999/10/09 00:01
CRDT- 1999/10/09 00:00
PHST- 1999/10/09 00:00 [pubmed]
PHST- 1999/10/09 00:01 [medline]
PHST- 1999/10/09 00:00 [entrez]
AID - 10.1074/jbc.274.42.30080 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 15;274(42):30080-6. doi: 10.1074/jbc.274.42.30080.