PMID- 10512881
OWN - NLM
STAT- MEDLINE
DCOM- 19991202
LR  - 20181113
IS  - 1059-1524 (Print)
IS  - 1059-1524 (Linking)
VI  - 10
IP  - 10
DP  - 1999 Oct
TI  - The EF-hand Ca(2+)-binding protein p22 associates with microtubules in an
      N-myristoylation-dependent manner.
PG  - 3473-88
AB  - Proteins containing the EF-hand Ca(2+)-binding motif, such as calmodulin and
      calcineurin B, function as regulators of various cellular processes. Here we
      focus on p22, an N-myristoylated, widely expressed EF-hand Ca(2+)-binding protein
      conserved throughout evolution, which was shown previously to be required for
      membrane traffic. Immunofluorescence studies show that p22 distributes along
      microtubules during interphase and mitosis in various cell lines. Moreover, we
      report that p22 associates with the microtubule cytoskeleton indirectly via a
      cytosolic microtubule-binding factor. Gel filtration studies indicate that the
      p22-microtubule-binding activity behaves as a 70- to 30-kDa globular protein. Our
      results indicate that p22 associates with microtubules via a novel
      N-myristoylation-dependent mechanism that does not involve classic
      microtubule-associated proteins and motor proteins. The association of p22 with
      microtubules requires the N-myristoylation of p22 but does not involve p22's
      Ca(2+)-binding activity, suggesting that the p22-microtubule association and the 
      role of p22 in membrane traffic are functionally related, because
      N-myristoylation is required for both events. Therefore, p22 is an excellent
      candidate for a protein that can mediate interactions between the microtubule
      cytoskeleton and membrane traffic.
FAU - Timm, S
AU  - Timm S
AD  - Department of Biology, University of Virginia, Charlottesville, Virginia 22903,
      USA.
FAU - Titus, B
AU  - Titus B
FAU - Bernd, K
AU  - Bernd K
FAU - Barroso, M
AU  - Barroso M
LA  - eng
GR  - R01 GM057519/GM/NIGMS NIH HHS/United States
GR  - R01-GM57519/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Biol Cell
JT  - Molecular biology of the cell
JID - 9201390
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Lipoproteins)
RN  - 0 (Microtubule-Associated Proteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Recombinant Proteins)
RN  - 0 (calcium binding protein p22, rat)
RN  - 0I3V7S25AW (Myristic Acid)
RN  - 451W47IQ8X (Sodium Chloride)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Calcium-Binding Proteins/genetics/*metabolism
MH  - Cell Cycle
MH  - Cell Line
MH  - Cytosol/metabolism
MH  - *EF Hand Motifs
MH  - Fluorescent Antibody Technique
MH  - Lipoproteins/genetics/*metabolism
MH  - Microtubule-Associated Proteins/metabolism
MH  - Microtubules/*metabolism/ultrastructure
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Myristic Acid/*metabolism
MH  - Peptide Fragments/immunology
MH  - Protein Binding
MH  - Rats
MH  - Recombinant Proteins
MH  - Sodium Chloride/pharmacology
PMC - PMC25618
EDAT- 1999/10/08 00:00
MHDA- 1999/10/08 00:01
CRDT- 1999/10/08 00:00
PHST- 1999/10/08 00:00 [pubmed]
PHST- 1999/10/08 00:01 [medline]
PHST- 1999/10/08 00:00 [entrez]
AID - 10.1091/mbc.10.10.3473 [doi]
PST - ppublish
SO  - Mol Biol Cell. 1999 Oct;10(10):3473-88. doi: 10.1091/mbc.10.10.3473.