PMID- 10531344
OWN - NLM
STAT- MEDLINE
DCOM- 19991216
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 44
DP  - 1999 Oct 29
TI  - A novel alternatively spliced variant of synaptotagmin VI lacking a transmembrane
      domain. Implications for distinct functions of the two isoforms.
PG  - 31428-34
AB  - Synaptotagmins are a family of membrane proteins that are characterized by a
      single transmembrane region and tandem C2 domains and that are likely to regulate
      constitutive and/or regulated vesicle traffic. We have shown that a subclass of
      synaptotagmins (III, V, VI, and X) forms homo- and heterodimers through an
      evolutionarily conserved cysteine motif at their N termini (Fukuda, M., Kanno,
      E., and Mikoshiba, K. (1999) J. Biol. Chem. 274, 31421-31427). In this study, we 
      identified a novel alternatively spliced variant of synaptotagmin (Syt) VI that
      lacks the N-terminal 85 amino acids including the transmembrane region (thus
      designated as Syt VIDeltaTM). Because it lacks the cysteine motif responsible for
      self-dimerization, Syt VIDeltaTM could not associate with Syt VI even in the
      presence of Ca(2+). Despite lacking the transmembrane region, Syt VIDeltaTM can
      associate with the plasma membrane through the C-terminal 29 amino acids. In
      adult mouse brain, two closely comigrating bands at M(r) approximately 50,000,
      which closely corresponded to the molecular weight of recombinant Syt VIDeltaTM, 
      were detected by anti-Syt VI antibody. These immunoreactive bands were found in
      both soluble and membrane fractions of mouse brain, indicating that they are
      membrane-associated proteins (Syt VIDeltaTM), but not transmembrane proteins (Syt
      VI). Expression of Syt VI and Syt VIDeltaTM in PC12 or COS-7 cells indicated that
      the two molecules have a distinct subcellular distribution: Syt VIDeltaTM is
      present in the cytosol or is associated with the plasma membrane or internal
      membrane structures, whereas Syt VI is localized to the endoplasmic reticulum
      and/or Golgi-like perinuclear compartment. These results suggest that Syt VI and 
      Syt VIDeltaTM may play distinct roles in vesicular trafficking.
FAU - Fukuda, M
AU  - Fukuda M
AD  - Developmental Neurobiology Laboratory, Brain Science Institute, Institute of
      Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako, Saitama 351-0198,
      Japan. mnfukuda@brain.riken.go.jp
FAU - Mikoshiba, K
AU  - Mikoshiba K
LA  - eng
SI  - GENBANK/AB026809
SI  - GENBANK/AB026810
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 (Calcium-Binding Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Protein Isoforms)
RN  - 0 (Syt6 protein, mouse)
RN  - 0 (Syt6 protein, rat)
RN  - 134193-27-4 (Synaptotagmins)
SB  - IM
MH  - *Alternative Splicing
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - *Calcium-Binding Proteins
MH  - Cell Compartmentation
MH  - Cell Membrane/chemistry
MH  - Cytosol/chemistry
MH  - Endoplasmic Reticulum/chemistry
MH  - Intracellular Membranes/chemistry
MH  - Membrane Glycoproteins/*genetics/isolation & purification/metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/*genetics/isolation & purification/metabolism
MH  - PC12 Cells
MH  - Protein Binding
MH  - Protein Isoforms
MH  - Rats
MH  - Sequence Homology, Amino Acid
MH  - Synaptotagmins
EDAT- 1999/10/26 00:00
MHDA- 1999/10/26 00:01
CRDT- 1999/10/26 00:00
PHST- 1999/10/26 00:00 [pubmed]
PHST- 1999/10/26 00:01 [medline]
PHST- 1999/10/26 00:00 [entrez]
AID - 10.1074/jbc.274.44.31428 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 29;274(44):31428-34. doi: 10.1074/jbc.274.44.31428.