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Gene Review

Slmap  -  sarcolemma associated protein

Mus musculus

Synonyms: D330001L02Rik, Kiaa1601, Sarcolemmal membrane-associated protein, Sarcolemmal-associated protein, Slap, ...
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Disease relevance of Slmap


High impact information on Slmap

  • Our inability to produce cell lines that stably expressed Slap suggested that Slap inhibited cell growth [2].
  • Agents that specifically disrupt microtubules did not affect SLMAP association with centrosomes [3].
  • Anti-peptide antibodies directed against SLMAP N-terminal sequences showed colocalization with gamma-tubulin at the centrosomes at all phases of the cell cycle [3].
  • This observation suggests that lack of sarcolemma-associated dystrophin in Duchenne muscular dystrophy (DMD) muscle may result from enhanced degradation of truncated mutation products rather than their inability per se to associate with the sarcolemma [4].
  • The cardiac-specific expression of SLMAP isoforms that can be targeted to distinct subcellular membranes, self assemble, and interact with the myofibril suggests a potential role for this molecule in the structural arrangement of the E-C coupling apparatus [5].

Biological context of Slmap

  • Elevated levels of centrosomal SLMAP were found to be lethal, whereas mutants that lacked centrosomal targeting inhibited cell growth accompanied by an accumulation of cells at the G2/M phase of the cell cycle [3].
  • These results imply that regulated levels and the temporal induction of SLMAP isoforms are important for normal muscle development [6].

Anatomical context of Slmap

  • We have elucidated the genomic structure of a gene encoding the sarcolemmal membrane-associated protein (SLMAP), which encodes a 91 kDa polypeptide with a previously uncharacterized N-terminal sequence encompassing a forkhead-associated (FHA) domain that resides at the centrosome [3].
  • A novel isoform of sarcolemmal membrane-associated protein (SLMAP) is a component of the microtubule organizing centre [3].
  • The expression of SLMAP was developmentally regulated and its localization was distinctly apparent at the level of the membranes involved in regulating the E-C coupling mechanism [5].
  • Dysfunctional SMAs were found to specifically upregulate the expression of a 35-kDa isoform of sarcolemmal membrane-associated protein (SLMAP), which is a component of the excitation-contraction coupling apparatus and implicated in the regulation of membrane function in muscle cells [7].
  • Several SLMAP isoforms were expressed in the cardiac myocyte with unique COOH-terminal membrane anchors that could target this molecule to distinct subcellular membranes [5].

Other interactions of Slmap


Analytical, diagnostic and therapeutic context of Slmap

  • Real-time PCR revealed high SLMAP mRNA levels in the db/db microvasculature, which were markedly downregulated during COOH treatment but elevated again when drug therapy was discontinued [7].
  • We further investigated this issue by transiently expressing Slap by microinjection [2].


  1. Molecular phenotyping of the mouse ky mutant reveals UCP1 upregulation at the neuromuscular junctions of dystrophic soleus muscle. Blanco, G., Pritchard, C., Underhill, P., Breeds, S., Townsend, K.M., Greenfield, A., Brown, S.D. Neuromuscul. Disord. (2004) [Pubmed]
  2. Src-like adaptor protein (Slap) is a negative regulator of mitogenesis. Roche, S., Alonso, G., Kazlauskas, A., Dixit, V.M., Courtneidge, S.A., Pandey, A. Curr. Biol. (1998) [Pubmed]
  3. A novel isoform of sarcolemmal membrane-associated protein (SLMAP) is a component of the microtubule organizing centre. Guzzo, R.M., Sevinc, S., Salih, M., Tuana, B.S. J. Cell. Sci. (2004) [Pubmed]
  4. Independent localization of dystrophin N- and C-terminal regions to the sarcolemma of mdx mouse myofibres in vivo. Dunckley, M.G., Wells, K.E., Piper, T.A., Wells, D.J., Dickson, G. J. Cell. Sci. (1994) [Pubmed]
  5. Molecular properties of cardiac tail-anchored membrane protein SLMAP are consistent with structural role in arrangement of excitation-contraction coupling apparatus. Guzzo, R.M., Salih, M., Moore, E.D., Tuana, B.S. Am. J. Physiol. Heart Circ. Physiol. (2005) [Pubmed]
  6. Regulated expression and temporal induction of the tail-anchored sarcolemmal-membrane-associated protein is critical for myoblast fusion. Guzzo, R.M., Wigle, J., Salih, M., Moore, E.D., Tuana, B.S. Biochem. J. (2004) [Pubmed]
  7. Endothelial dysfunction in Type 2 diabetes correlates with deregulated expression of the tail-anchored membrane protein SLMAP. Ding, H., Howarth, A.G., Pannirselvam, M., Anderson, T.J., Severson, D.L., Wiehler, W.B., Triggle, C.R., Tuana, B.S. Am. J. Physiol. Heart Circ. Physiol. (2005) [Pubmed]
  8. Observations on the muscle plasma membrane-associated cytoskeletons of mdx mice by quick-freeze, deep-etch, rotary-shadow replica method. Wakayama, Y., Shibuya, S. Acta Neuropathol. (1990) [Pubmed]
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